Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Alexandre+Guichard Proteopedia - User contributions [en] 2026-10-06T02:18:58Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3144076 Sandbox Reserved 1108 2020-01-17T08:09:32Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> 4iv6 is an enzyme ''Mycobacterium tuberculosis'' which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight ''Mycobacterium tuberculosis'' relative infections.<br /> <br /> == Function ==<br /> 4iv6 functions were not studied and only structural infos are disponible.<br /> Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.<br /> E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:<br /> <br /> [[Analine metabolism]]:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&ecno=1.3.8.1]<br /> <br /> [[Butanoate metabolism]]:[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]<br /> <br /> [[Lipids metabolism]] : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]<br /> <br /> [[Valine Leucine and isoleucine pathways]]:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]<br /> <br /> <br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> <br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Informed Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if ''Mycobacterium tuberculosis'' gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''Mycobacterium tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights summary ==<br /> <br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/2asymunit/1'>Asymmetric units</scene><br /> <br /> <scene name='82/829361/Betasheetchaina_asymunit/1'>Beta-sheets</scene><br /> <br /> <scene name='82/829361/Helixalphachaina_asymunit/1'>Helices</scene><br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> <br /> <br /> <scene name='82/829361/Chainea_asymunit/2'>A chain</scene> <br /> <br /> <scene name='82/829361/Chaineb_asymunit/1'>B chain</scene><br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene><br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143934 Sandbox Reserved 1108 2020-01-16T19:49:35Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> 4iv6 is an enzyme ''Mycobacterium tuberculosis'' which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight ''Mycobacterium tuberculosis'' relative infections.<br /> <br /> == Function ==<br /> 4iv6 functions were not studied and only structural infos are disponible.<br /> Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.<br /> E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] is communly found in following pathways with various functions:<br /> <br /> Analine metabolism:[https://www.brenda-enzymes.info/pathway_index.php?pathway=alanine%20metabolism&ecno=1.3.8.1]<br /> Butanoate metabolism :[https://www.genome.jp/kegg-bin/show_pathway?map00650+1.3.8.1]<br /> Lipids metabolism : [https://www.brenda-enzymes.info/pathway_index.php?pathway=lipid%20metabolism&ecno=1.3.8.1][https://www.genome.jp/kegg-bin/show_pathway?map00071+1.3.8.1]<br /> Valine Leucine and isoleucine pathways:[https://www.genome.jp/kegg-bin/show_pathway?map00280+1.3.8.1]<br /> <br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> <br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Informed Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if ''Mycobacterium tuberculosis'' gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''Mycobacterium tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights summary ==<br /> <br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/2asymunit/1'>Asymmetric units</scene><br /> <br /> <scene name='82/829361/Betasheetchaina_asymunit/1'>Beta-sheets</scene><br /> <br /> <scene name='82/829361/Helixalphachaina_asymunit/1'>Helices</scene><br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> <br /> <br /> <scene name='82/829361/Chainea_asymunit/2'>A chain</scene> <br /> <br /> <scene name='82/829361/Chaineb_asymunit/1'>B chain</scene><br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene><br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143923 Sandbox Reserved 1108 2020-01-16T19:16:31Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> 4iv6 is an enzyme ''Mycobacterium tuberculosis'' which get his structure analyzed by Baugh et al. [https://www.ncbi.nlm.nih.gov/pubmed/25613812] with other enzymes homologue in order to fight ''Mycobacterium tuberculosis'' relative infections.<br /> <br /> == Function ==<br /> 4iv6 functions were not studied and only structural infos are disponible.<br /> Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.<br /> Butyryl-CoA Dehydrogenase[https://meshb.nlm.nih.gov/record/ui?name=Short-chain%20acyl-CoA%20dehydrogenase].<br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> <br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Informed Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if ''Mycobacterium tuberculosis'' gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''Mycobacterium tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights summary ==<br /> <br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/2asymunit/1'>Asymmetric units</scene><br /> <br /> <scene name='82/829361/Betasheetchaina_asymunit/1'>Beta-sheets</scene><br /> <br /> <scene name='82/829361/Helixalphachaina_asymunit/1'>Helices</scene><br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> <br /> <br /> <scene name='82/829361/Chainea_asymunit/2'>A chain</scene> <br /> <br /> <scene name='82/829361/Chaineb_asymunit/1'>B chain</scene><br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene><br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143920 Sandbox Reserved 1108 2020-01-16T19:05:02Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> 4iv6 functions were not studied and only structural infos are disponible.<br /> Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.<br /> Butyryl-CoA Dehydrogenase[https://meshb.nlm.nih.gov/record/ui?name=Short-chain%20acyl-CoA%20dehydrogenase].<br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> <br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Informed Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights summary ==<br /> <br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/2asymunit/1'>Asymmetric units</scene><br /> <br /> <scene name='82/829361/Betasheetchaina_asymunit/1'>Beta-sheets</scene><br /> <br /> <scene name='82/829361/Helixalphachaina_asymunit/1'>Helices</scene><br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> <br /> <br /> <scene name='82/829361/Chainea_asymunit/2'>A chain</scene> <br /> <br /> <scene name='82/829361/Chaineb_asymunit/1'>B chain</scene><br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene><br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143909 Sandbox Reserved 1108 2020-01-16T18:47:41Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> 4iv6 functions were not studied and only structural infos are disponible.<br /> Nevertheless we can consider datas from other E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1] which came from other organisms.<br /> Butyryl-CoA Dehydrogenase[https://meshb.nlm.nih.gov/record/ui?name=Short-chain%20acyl-CoA%20dehydrogenase].<br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Informed Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene> :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene> : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143199 Sandbox Reserved 1108 2020-01-14T19:11:18Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> ==Enzymatic reaction<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4iv6</ref><ref>https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.3.8.1</ref><ref>https://enzyme.expasy.org/EC/1.3.8.1</ref>==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene> :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene> : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3143197 Sandbox Reserved 1108 2020-01-14T19:07:14Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==4iv6==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure<ref>http://www.rcsb.org/structure/4IV6</ref>==<br /> <br /> Isovaleryl-CoA dehydrogenase is the assembly of '''<scene name='82/829361/2asymunit/1'>two asymmetric units</scene>''' each composed of '''two chains <scene name='82/829361/Chainea_asymunit/2'>A</scene> and <scene name='82/829361/Chaineb_asymunit/1'>B</scene>''' linked by a <scene name='82/829361/Ligand_asymunit/1'>ligand</scene> (Dihydroflavine-Adenine Dinucleotide also known as [https://pubchem.ncbi.nlm.nih.gov/compound/Dihydroflavine-adenine-dinucleotide FADH2] ). Each of the two chains A and B are composed of 388 amino acids. An asymmetric unit is therefore composed of 776 amino acids and has a molecular weight of 86233.70 Da.<br /> <br /> The A chain is made up of <scene name='82/829361/Helixalphachaina_asymunit/1'>17 helices</scene> (involving 221 residues) and <scene name='82/829361/Betasheetchaina_asymunit/1'>14 beta-sheets</scene> (61 residues).<br /> Chain B is formed of <scene name='82/829361/Helixchainb_asymunit/1'>17 helices</scene> (involving 218 residues) and <scene name='82/829361/Betasheetchainb_asymunit/1'>14 beta-sheets</scene> (62 residues). <br /> <br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene> :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene> : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142713 Sandbox Reserved 1108 2020-01-12T16:16:01Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene> :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <scene name='82/829361/Hydrophobic/1'>Hydrophobic region</scene> : Green: FDA, Purple: Polar region, Light grey: Hydrophobic region <br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142697 Sandbox Reserved 1108 2020-01-12T15:48:44Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene> :Light Grey:1st sub-unit, Light green:2nd sub-unit, Blue and red:FDA <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142696 Sandbox Reserved 1108 2020-01-12T15:45:20Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/2'>Asymetrical unit</scene><br /> <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142692 Sandbox Reserved 1108 2020-01-12T15:41:03Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene> : Red: helix alpha, Blue:FDA, Yellow: Beta sheet <br /> <br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142689 Sandbox Reserved 1108 2020-01-12T15:33:04Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> <scene name='82/829361/Asymetrical_unit/1'>Asymetrical unit</scene><br /> <br /> <scene name='82/829361/Secondary_structure/1'>Secondary structure</scene><br /> <br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142688 Sandbox Reserved 1108 2020-01-12T15:25:59Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <scene name='82/829361/Asymetrical_unit/1'>Asymetrical unit</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142686 Sandbox Reserved 1108 2020-01-12T15:23:58Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <scene name='82/829361/Biological_unit/1'>Biological unit</scene><br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142673 Sandbox Reserved 1108 2020-01-12T14:53:52Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1[https://enzyme.expasy.org/EC/1.3.8.1]<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3142671 Sandbox Reserved 1108 2020-01-12T14:49:30Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> <br /> [[Enzyme accepted name]]: Short-chain acyl-CoA dehydrogenase<br /> <br /> [[Other names]]:Butanoyl-CoA dehydrogenase, Butyryl dehydrogenase, Short-chain acyl CoA dehydrogenase, Unsatured acyl-CoA reductase.<br /> <br /> [[Enzyme class]]: E.C.1.3.8.1 (Lien clickable: https://enzyme.expasy.org/EC/1.3.8.1 )<br /> <br /> [[Substrate]]: A short-chain acyl CoA <br /> <br /> [[Prosthetic group]]: 1 electron-transfer flavoprotein such as FDA, for every Subunits <br /> <br /> [[Products]]: a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein<br /> <br /> [[Pathways]]: Fatty acid degradation<br /> <br /> [[Other information]]:<br /> <br /> The enzyme from beef liver can accept acyl-chain lengths from 3 to 8 carbon atoms. From different organism the range can vary so we ignore if M.tuberculosis gets the same lengths resolution.<br /> <br /> The highest activity reported for beef liver enzyme was for substrates with 4 and 5 carbon acyl-chain lengths.<br /> <br /> ==4IV6 as a research tool==<br /> <br /> 4iv6 which belong to ''Mycobacterium tuberculosis'' was studied with other protein homolog.<br /> They were chosen to be studied as potential TB-Drugs target<br /> Studies have been made on homolog similarities aimed on their active site because with the knowledges of many homolog active site structure and how they work, we can design a inhibitor of those enzyme which can stop essential reaction and reduce or stop ''M.tuberculosis'' infection.<br /> This strategy is called an « Homolog-rescue strategy ».<br /> This strategy can be generalized for other drug target for other diseases.<br /> <br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard https://proteopedia.org/index.php?title=Sandbox_Reserved_1108&diff=3122552 Sandbox Reserved 1108 2019-12-05T20:44:23Z

<p>Alexandre Guichard: </p> <hr /> <div>{{Sandbox_ESBS_2019}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> ==Primary and Secondary structure==<br /> ==Tertiary structures==<br /> ==Enzymatic reaction==<br /> ==4IV6 as a research tool==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> <references/></div>

Alexandre Guichard