Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Jah+Ia+Yang Proteopedia - User contributions [en] 2026-09-24T09:35:46Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873723 Sandbox Reserved 772 2013-12-07T05:05:23Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199<http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf></ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">J. Pascale, M. Abdo, R. Boigegrain, J. Montero, J. Winum, S. Kohler. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199<http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf></ref> '' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">Turtaut, Francois, Safia Ouahrani-Bettache, Jean Montero, Stephan Kohler, and Jean-Yves Winum. "Synthesis and Biological Evaluation of a New Class of Anti-brucella Compounds Targeting Histidinol Dehydrogenase: α-O-arylketones and α-S-arylketones Derived from Histidine." Med. Chem. Commun. 2(2011): 995-1000. Web. 27 Nov. 2013. <http://pubs.rsc.org.prox.lib.ncsu.edu/en/Content/ArticleLanding/2011/MD/c1md00146a#!divCitation>.</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873722 Sandbox Reserved 772 2013-12-07T05:03:25Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199<http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf></ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">J. Pascale, M. Abdo, R. Boigegrain, J. Montero, J. Winum, S. Kohler. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">Turtaut, Francois, Safia Ouahrani-Bettache, Jean Montero, Stephan Kohler, and Jean-Yves Winum. "Synthesis and Biological Evaluation of a New Class of Anti-brucella Compounds Targeting Histidinol Dehydrogenase: α-O-arylketones and α-S-arylketones Derived from Histidine." Med. Chem. Commun. 2(2011): 995-1000. Web. 27 Nov. 2013. <http://pubs.rsc.org.prox.lib.ncsu.edu/en/Content/ArticleLanding/2011/MD/c1md00146a#!divCitation>.</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873718 Sandbox Reserved 772 2013-12-07T04:58:13Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">J. Pascale, M. Abdo, R. Boigegrain, J. Montero, J. Winum, S. Kohler. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873716 Sandbox Reserved 772 2013-12-07T04:55:01Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">Joseph, Pascale. "Targeting of the Brucella Suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen." American Society for Microbiology (2007): N. pag. Web. 27 Nov. 2013. <http://aac.asm.org/content/51/10/3752.short>.</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873714 Sandbox Reserved 772 2013-12-07T04:53:14Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.short</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873712 Sandbox Reserved 772 2013-12-07T04:49:36Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">PNAS 2002 99 (4) 1859-1864; published ahead of print February 12, 2002, doi:10.1073/pnas.022476199</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873701 Sandbox Reserved 772 2013-12-07T04:38:47Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873697 Sandbox Reserved 772 2013-12-07T04:36:26Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.<ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref>' /> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873692 Sandbox Reserved 772 2013-12-07T04:35:25Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /> <ref name="pymol">The JyMOL Molecular Graphics System, Version 1.0, Schrödinger, LLC.</ref> <br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873690 Sandbox Reserved 772 2013-12-07T04:33:55Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> <br /> [[Image:Monomer.gif |300px]]<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Figure 1.''' ''(A) Stereo view of the monomer. Domains: 1, blue; 2, green; 3, orange; 4, magenta. L-histidinol, NAD, and the Zn2� are shown as ball-and-sticks. ( B) Domain 1. Rossmann fold shown in blue, V-shaped pairs of helices (residues 25 –103) connected by a linker that forms the sixth strand are in cyan. (C) Domain 2. Rossmann fold (green) in similar orientation as B. Strand-helix hairpin completes the �-sheet (residues 1–24, magenta). (D) Topology diagram. Secondary structure elements are numbered consecutively. The chain meanders between domains in the order 2 –1-3–1-2–1-3– 4. (E) HisD dimer with one molecule colored as in A and the other shown in pale colors. Zn2� atoms and NAD bound to each monomer (red) define the position of the active site.'' <br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> '''Figure. 2''' ''This is the full sequence of histidinol dehydrogenase.''<br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> '''Figure 3.''' ''This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>'' <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873682 Sandbox Reserved 772 2013-12-07T04:27:41Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains, two larger domains and two smaller domains. The two larger domains make up the globule and the two smaller domains make up the extending tail. The intertwined dimer is thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> [[Image:Monomer.gif |300px]]<br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=File:Monomer.gif&diff=1873681 File:Monomer.gif 2013-12-07T04:26:47Z

<p>Jah Ia Yang: </p> <hr /> <div></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873663 Sandbox Reserved 772 2013-12-07T04:11:51Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/2'>A</scene>, <scene name='56/564048/Chain_b/2'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873650 Sandbox Reserved 772 2013-12-07T04:05:06Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': <scene name='56/564048/Chain_a/1'>A</scene>, <scene name='56/564048/Chain_b/1'>B</scene> <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873615 Sandbox Reserved 772 2013-12-07T03:41:41Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The crystal structure of histidinol dehydrogenase can be determined by x-ray crystallography. The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH functions as a homodimer, but it consists of two monomers. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the two main active sites of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1873580 Sandbox Reserved 772 2013-12-07T03:20:16Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the active sites (proton acceptors) of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is as follows:<br /> <br /> -1 proton and 1 hydride are abstracted from L-histidinol by His-327 (B1). NAD+ accepts hydride.<br /> <br /> -L-histdinol becomes L-histidinaldehyde (sp2)<br /> <br /> -Reduced NADH cofactor leaves and then is replaced by another NAD+<br /> <br /> -Water is activated by Glu-326 (B2) and makes a nucleophilic attack on the reactive carbon.<br /> <br /> -Concurrently, His-327 (B3) donates its proton to the aldehyde oxygen<br /> <br /> -Repeat step 1 and then it leads to the formation of L-histidine <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase is an amino acid biosynthetic enzyme, which can provide a novel target for the development of anti-Brucella agents. Histidinol dehydrogenase has no counterpart in mammalians; therefore, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870341 Sandbox Reserved 772 2013-12-03T16:02:29Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HDH is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each HDH monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the active sites (proton acceptors) of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870335 Sandbox Reserved 772 2013-12-03T15:38:47Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. Brucellosis is a bacterial disease transmitted by having contact with infected animals. HDH being encoded by ''hisD'' is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> Because HDH is absent from mammals, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the active sites (proton acceptors) of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. It is a bacterial disease of human beings transmitted by contact with infected animals or infected meat or milk products. It causes fever and headaches. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870328 Sandbox Reserved 772 2013-12-03T14:53:07Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the active sites (proton acceptors) of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870327 Sandbox Reserved 772 2013-12-03T14:47:32Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x'/><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870326 Sandbox Reserved 772 2013-12-03T14:44:06Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''hisD'' in Brucellosis, commonly known as Maltafeve. This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': ''Escherichia coli'' (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870325 Sandbox Reserved 772 2013-12-03T14:43:05Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene ''his''D in Brucellosis, commonly known as Maltafeve. This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870324 Sandbox Reserved 772 2013-12-03T14:42:26Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> HDH is encoded by the structural gene hisD in Brucellosis, commonly known as Maltafeve. This is essential for intramacrophagic replication because it provides a novel target for the development of anti-Brucella agent.<ref name="article5">http://aac.asm.org/content/51/10/3752.full.pdf+html</ref> HDH is absent from mammals; therefore, it has become an attractive target for inhibition as part of the herbicide development.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870323 Sandbox Reserved 772 2013-12-03T14:29:33Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme that catalyzes the last step in the histidine biosynthetic pathway, which converts L-histidinol to L-histidine with a L-histidinaldehyde intermediate. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. HDH has been one of the most studied enzyme biochemically and genetically throughout time. HDH is encoded by the structural gene hisD. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870322 Sandbox Reserved 772 2013-12-03T14:21:45Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. The catalyzation of the last step in the biosynthetic pathway of histidine, causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870321 Sandbox Reserved 772 2013-12-03T14:02:53Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' scene='x' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870320 Sandbox Reserved 772 2013-12-03T13:56:27Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='The crystal structure shows a functional homodimer in the asymmetric unit.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref>' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870319 Sandbox Reserved 772 2013-12-03T13:52:31Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': glycerol ([http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL]), selenomethionine ([http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE]), sulfate ion ([http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4])<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref><br /> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870318 Sandbox Reserved 772 2013-12-03T13:46:05Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule<br /> <br /> The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870317 Sandbox Reserved 772 2013-12-03T13:25:13Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues).<ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), and the intertwined dimer was thought to result from domain swapping. The two domains presents a similar incomplete Rossmann fold, which suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site (residue His-327) participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870316 Sandbox Reserved 772 2013-12-03T13:16:08Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |left|250px]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png |300px]]]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870315 Sandbox Reserved 772 2013-12-03T12:49:23Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870314 Sandbox Reserved 772 2013-12-03T12:46:17Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is an enzyme coded by the structural gene hisD. HDH catalyzes the last step in the histidine biosynthetic pathway. This primordial pathway was found in bacteria, archaebacteria, fungi, and plants. hiD catalyzes the last step in the biosynthetic pathway of histidine, which causes the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], MSE[http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870313 Sandbox Reserved 772 2013-12-03T12:24:42Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH''' <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> [[Image:403px-Histidine decarboxylase seq.png]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870259 Sandbox Reserved 772 2013-12-03T03:55:24Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> '''Sequence of HDH'''<br /> [[Image:403px-Histidine decarboxylase seq.png]]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> 1. extraction of one proton and one hydride from L-histidinol<br /> <br /> 2. reduced NADH leaves and replaced by NAD+<br /> <br /> 3. repeat the first step<br /> <br /> 4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> 5. formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=File:403px-Histidine_decarboxylase_seq.png&diff=1870258 File:403px-Histidine decarboxylase seq.png 2013-12-03T03:39:40Z

<p>Jah Ia Yang: </p> <hr /> <div></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870257 Sandbox Reserved 772 2013-12-03T03:36:39Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> -extraction of one proton and one hydride from L-histidinol[1]<br /> <br /> -reduced NADH leaves and replaced by NAD+<br /> <br /> -repeat the first step<br /> <br /> -His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> -formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870256 Sandbox Reserved 772 2013-12-03T03:34:41Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <br /> The process is as follows:<br /> <br /> -extraction of one proton and one hydride from L-histidinol[1]<br /> <br /> -reduced NADH leaves and replaced by NAD+<br /> <br /> -repeat the first step<br /> <br /> -His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> <br /> -formation of l-histidine<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870255 Sandbox Reserved 772 2013-12-03T03:32:49Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. The process is as follows:<br /> -extraction of one proton and one hydride from L-histidinol[1]<br /> -reduced NADH leaves and replaced by NAD+<br /> -repeat the first step<br /> -His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride<br /> -formation of l-histidine.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870253 Sandbox Reserved 772 2013-12-03T03:08:09Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. <br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870251 Sandbox Reserved 772 2013-12-03T03:02:12Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Histidinol dehydrogenase being exclusively necessary for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens for Brucellosis. Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella.<ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870249 Sandbox Reserved 772 2013-12-03T02:56:54Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> The overall structure is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. <br /> <br /> The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being essential exclusively for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens. <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870245 Sandbox Reserved 772 2013-12-03T02:48:09Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. <br /> <br /> The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being essential exclusively for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens. <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870244 Sandbox Reserved 772 2013-12-03T02:47:29Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages. <br /> <br /> The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. <br /> <br /> The virulome analysis of Brucella suis shows that genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. Histidinol dehydrogenase being essential exclusively for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<br /> <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870238 Sandbox Reserved 772 2013-12-03T01:47:40Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, most commonly known as Maltafever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp., is a facultative intracellular pathogen developed inside the host’s macrophages.<br /> <br /> Pathogenesis is linked to this intramacrophagic replication. Due to its intracellular localization, eradication of Brucella spp. with standard chemotherapy strategies such as antibiotic treatment is delicate. <br /> <br /> Moreover, clinical isolates show that drug-resistant Brucella strains are developing. The absence of a vaccine for humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new therapeutic strategies to eradicate this reemerging pathogen. <br /> <br /> The virulome analysis of Brucella suis has shown that among others, genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria.<br /> <br /> This new approach consists in targeting a virulence factor of this pathogen, the histidinol dehydrogenase (HDH, EC. 1.1.23). 5–7 <br /> <br /> This metalloenzyme is involved in the final two steps of the biosynthesis of histidine where it catalyses the NAD dependent oxidation of histidinol to histidine via histidinaldehyde.<br /> <br /> Inhibition of its enzymatic activity with specific inhibitors will prevent intramacrophagic multiplication of Brucella. HDH being essential exclusively for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens.<br /> <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870234 Sandbox Reserved 772 2013-12-03T01:38:53Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Km''': <br /> <br /> '''Vmax''': <br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis, most commonly known as Malta fever or undulant fever, is the most widespread bacterial zoonosis worldwide. Its causative agent, Brucella spp. , is a facultative intracellular pathogen developing inside the host’s macrophages, and patho-genesis is linked to this intramacrophagic replication. Due to its intracellular localization, eradication of Brucella spp. with stan-dard chemotherapy strategies such as antibiotic treatment is delicate.<br /> Moreover, clinical isolates show that drug-resistant Brucella strains are developing. The absence of a vaccine for<br /> humans and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new<br /> therapeutic strategies to eradicate this reemerging pathogen. The virulome analysis of Brucella suishas shown that among others, genes involved in the biosynthesis of amino acids are essential for the virulence of the bacteria. This new approach consists in targeting a virulence factor of this pathogen, the histidinol dehydrogenase (HDH, EC. 1.1.23). This metalloenzyme is involved in the final two steps of the biosynthesis of histidine where it catalyses the NAD dependent oxidation of histidinol to histidine via histidinaldehyde. Inhibition of its enzymatic activity<br /> with specific inhibitors will prevent intramacrophagic multipli-cation of Brucella. HDH being essential exclusively for the growth of the bacteria inside the macrophage of the host, and having no counterpart in mammalians, it constitutes a therapeutic target for the development of an anti-infectious treatment against intracellular pathogens. <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870232 Sandbox Reserved 772 2013-12-03T01:35:54Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Km''': <br /> <br /> '''Vmax''': <br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> ==Implications or Possible Applications==<br /> Brucellosis,<br /> 1<br /> most commonly known as Malta fever or undulant<br /> fever, is the most widespread bacterial zoonosis worldwide. Its<br /> causative agent, Brucella spp. , is a facultative intracellular<br /> pathogen developing inside the host’s macrophages, and patho-genesis is linked to this intramacrophagic replication. Due to its<br /> intracellular localization, eradication of Brucella spp. with stan-dard chemotherapy strategies such as antibiotic treatment is<br /> delicate.<br /> 2<br /> Moreover, clinical isolates show that drug-resistant<br /> Brucella strains are developing. The absence of a vaccine for<br /> humans<br /> 3<br /> and the appearing resistance of Brucella spp. to anti-biotic chemotherapy points to the necessity to develop new<br /> therapeutic strategies to eradicate this reemerging pathogen. The<br /> virulome analysis of Brucella suishas shown that among others,<br /> genes involved in the biosynthesis of amino acids are essential for<br /> the virulence of the bacteria.<br /> 4<br /> This new approach consists in<br /> targeting a virulence factor of this pathogen, the histidinol<br /> dehydrogenase (HDH, EC. 1.1.23).<br /> 5–7<br /> This metalloenzyme is<br /> involved in the final two steps of the biosynthesis of histidine<br /> where it catalyses the NAD dependent oxidation of histidinol to<br /> histidine via histidinaldehyde. Inhibition of its enzymatic activity<br /> with specific inhibitors will prevent intramacrophagic multipli-cation of Brucella. HDH being essential exclusively for the<br /> growth of the bacteria inside the macrophage of the host, and<br /> having no counterpart in mammalians, it constitutes<br /> a therapeutic target for the development of an anti-infectious<br /> treatment against intracellular pathogens. <ref name="article2">http://pubs.rsc.org.prox.lib.ncsu.edu/en/content/articlepdf/2011/md/c1md00146a</ref><br /> <br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870227 Sandbox Reserved 772 2013-12-03T01:25:40Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref><br /> <br /> '''Km''': <br /> <br /> '''Vmax''': <br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870222 Sandbox Reserved 772 2013-12-03T01:20:02Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref><br /> <br /> '''Molecular Weight''': <br /> <br /> '''Isoelectric Point''': <br /> <br /> '''Km''': <br /> <br /> '''Vmax''': <br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> <br /> For the overall structure, it is 48% helical (20 helices; 211 residues) and 16% beta sheet (15 strands; 73 residues). <ref name="structure">http://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=1K75&bionumber=1</ref> <br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref><br /> ==References== <br /> <references /></div>

Jah Ia Yang https://proteopedia.org/index.php?title=Sandbox_Reserved_772&diff=1870220 Sandbox Reserved 772 2013-12-03T01:08:18Z

<p>Jah Ia Yang: </p> <hr /> <div><br /> {{User:Michael_B._Goshe/Template_BCH455_555}}<br /> <br /> <br /> <br /> <Structure load='1K75' size='500' frame='true' align='right' caption='INSERT CAPTION HERE' scene='Insert optional scene name here' /><br /> <br /> <br /> [[Image:PDB_1k75_EBI.jpg |thumb |this is a caption ]]<br /> <br /> ==Histidinol Dehydrogenase==<br /> <br /> Histidinol dehydrogenase (HDH) is coded by the structural gene hisD. Histidinol dehydrogenase catalyzes the last step in the histidine biosynthetic pathway. This pathway was found in bacteria, archaebacteria, fungi, and plants. The pathway involves the conversion of L-histidinol to L-histidine with a L-histidinaldehyde intermediate <ref name="rasmol">citation</ref><br /> <br /> <br /> __TOC__<br /> <br /> ==General Information==<br /> <br /> '''Gene Name''': hisD <ref name="info">citation5</ref><br /> <br /> '''Organism''': Escherichia coli (strain K12) <ref name="info">citation5</ref><br /> <br /> '''Classification''': Oxidoreductase<br /> <br /> '''Length''': 434 Amino Acids <ref name="info">citation5</ref> <br /> <br /> '''Chains''': A, B <ref name="cite2">cite2</ref><br /> <br /> '''Molecular Weight''': <br /> <br /> '''Isoelectric Point''': <br /> <br /> '''Km''': <br /> <br /> '''Vmax''': <br /> <br /> ==Structure==<br /> <br /> HisD is a monomer, but it functions as a homodimer. The presence of Zn2+ cation is required per monomer. Each hisD monomer is made of four domains,two larger domains (globule) and two smaller domains (extending tail), whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. The active site, residue His-327, participates in acid-base catalysis <ref name="rasmol">CITATION</ref><br /> <br /> 48% helical (20 helices; 211 residues)<br /> 16% beta sheet (15 strands; 73 residues)<br /> <br /> <br /> <br /> '''Related Structures''': [http://proteopedia.org/wiki/index.php/1kae 1KAE] and [http://proteopedia.org/wiki/index.php/1kar 1KAR]<br /> <br /> ==Enzymatic Mechanism==<br /> <br /> [[Image:pathways.jpg]]<br /> <br /> This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. <ref name="rasmol">1</ref><br /> ==References== <br /> <references /></div>

Jah Ia Yang