Proteopedia - User contributions [en]

Phosphoglucoisomerase

2010-04-02T12:34:34Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a monomer molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site2/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1.''' The substrate binds to the enzyme.

'''Step 2.''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3.''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4.''' Glu357 donates back the proton at the C1 position.

'''Step 5.''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- Phosphoglucoisomerase is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>

[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-29T01:43:51Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a monomer molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1.''' The substrate binds to the enzyme.

'''Step 2.''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3.''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4.''' Glu357 donates back the proton at the C1 position.

'''Step 5.''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- Phosphoglucoisomerase is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>

[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-29T01:23:45Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1.''' The substrate binds to the enzyme.

'''Step 2.''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3.''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4.''' Glu357 donates back the proton at the C1 position.

'''Step 5.''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- Phosphoglucoisomerase is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>

[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-28T00:57:51Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1.''' The substrate binds to the enzyme.

'''Step 2.''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3.''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4.''' Glu357 donates back the proton at the C1 position.

'''Step 5.''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- Phosphoglucoisomerase is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>
[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-28T00:49:41Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- Phosphoglucoisomerase is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>
[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-28T00:47:22Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/2'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- it was found that PGI is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>
[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-28T00:27:20Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the reversible conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- it was found that PGI is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of PGI does depend on the pH and temperature of the environment.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>
[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-28T00:24:26Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

'''Regulation'''- it was found that PGI is regulated only by the relative concentrations of glucose-6-phosphate and fructose 6-phosphate, towards equilibrium. Nevertheless, it was found that the kinetic parameters of the PGI does depend on the pH and temperature of the environment it is found in.
The following kinetic parameters are proposed for rabbit PGI at pH 8.5 and 30°C <ref>PMID: 5647261</ref>
[[Image:Kinetic_PGI.JPG]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

File:Kinetic PGI.JPG

2010-03-28T00:08:49Z

Bogdan Stancu: PGI Kinetic Parameters

== Summary ==
PGI Kinetic Parameters
== Licensing ==
{{self|cc-by-sa-3.0}}

Phosphoglucoisomerase

2010-03-27T22:42:54Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate. This reaction is driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor. Secreted by T cells, promotes the survival of certain sensory and embryonic nerve cells. Also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation. A "hook" that can potentially be involved in the previously mentioned extracellular activities.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a small movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.

[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T15:12:52Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T04:00:59Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera--a visualization system for exploratory research and analysis. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]
Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:59:46Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell <ref>PMID:11371164</ref>.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)<ref> UCSF Chimera--a visualization system for exploratory research and analysis. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. J Comput Chem. 2004 Oct;25(13):1605-12. </ref>]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another characteristic trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation.

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red for highly conserved regions - dark blue for variable reigions) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]
Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in '''Figure 2''' as change in the position of an α helix.

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]])

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:46:50Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="400" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:45:40Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="500" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|left|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:44:57Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="500" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:42:09Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.<ref> Voet D, Voet J, and Pratt C. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref>

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:32:52Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

'''Step 1''' The substrate binds to the enzyme.

'''Step 2''' The residue Lys518 (or His388b) acts as an enzymatic acid catalyzing the opening of the ring.

'''Step 3''' Conserved Glu357 abstracts the acidic proton from C2 forming a cis-enendiol intermediate.

'''Step 4''' Glu357 donates back the proton at the C1 position.

'''Step 5''' Lys518 (or His388b) abstracts back the proton from the sugar ring oxygen, resulting in a ring closure, to give the product.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:22:09Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

Step 1 The substrate binds to the enzyme.
Step 2 The residue Lys518 or His388b acts as an enzymatic acid catalazyng the opening of the ring.
[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:18:08Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (blue)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:17:38Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Figure 1.''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (turquoise)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Figure 2.''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:16:33Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Fig.1''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (turquoise)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).

Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.
[[Image:Active_site_movement.jpg|thumb|right|'''Fig.2''' Substrate induced movement]]

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-03-01T03:15:52Z

Bogdan Stancu: /* '''Structure''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Human phosphoglucose isomerase (1IAT)" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin <ref>PMID:3764429</ref>.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis<ref>PMID:12054796</ref>.
* Maturation factor(MF) <ref>PMID:8639816</ref>
* Myofibril-bound serine protese inhibitor (MBSPI)<ref>PMID:10833440</ref>

=='''Structure'''==
<applet load="1hox" size="300" color="white" frame="true" align="right" caption="Phosphoglucose isomerase" />
[[Image:Align.jpg|thumb|left|'''Fig.1''' Multiple alignment PGI - ''Geobacillus stearothermophilus'' (white),'' Homo sapiens'' (pink), ''Oryctolagus cuniculus'' (turquoise)]]

Phosphoglucose isomerase exists in the cell usually as a <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Dimer/1'>homodimer</scene>, nevertheless outside of the cell, it has been isolated as <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Monomer/1'>monomeric</scene> structure. PGI has essentially an identical fold in all of the characterized species (see '''Figure 1'''). The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Sec_struct/1'>secondary structure</scene> of phosphoglucose isomerase is charaterized by an αβα conformation, on each of its two domains. The smaller domain is characterized by 5 parallel β-sheets, while the larger domain if formed out of 6 parallel/antiparallel β-sheets. Furthermore, another charateristical trait is a residue extension at the C-terminus, which wraps around the other monomer in the dimeric conformation

Phosphoglucose isomerase has a molecular mass of proximately 55 kDa.

'''Active Site''' - Mammalian PGI shows a degree of <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Conservation2/1'>conservation</scene> ( dark red represent highly conserved regions - dark blue regions that are variable) of about 90 %. The <scene name='Stancu_Phosphoglucoisomerase_Sandbox_1/Active_site/1'>active site</scene> is the region with highest observed conservation, with a number of residues that are crucial in the mechanism of the enzyme (Lys210, Gln353, Glu357, Gln511, Lys518, His388b).
[[Image:Active_site_movement.jpg|thumb|left|'''Fig.2''' Substrate induced movement]]
Another characteristic of phosphoglucose isomerase is that binding of substrate at the active site, induces a movement in the conformation of the enzyme. This can be seen in Figure 2 as change in the position of an α helix.

=='''Mechanism'''==
The proposed reaction mechanism of PGI for the conversion of glucose-6-phosphate to fructose 6-phosphate involves an acid/base catalysis by the enzyme.

[[Image:Mech.png]]

=='''Links'''==

* Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

* Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

* Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

File:Active site movement.jpg

2010-03-01T03:14:42Z

Bogdan Stancu: Substrate induced movement

== Summary ==
Substrate induced movement
== Licensing ==
{{self|cc-by-3.0}}

Phosphoglucoisomerase

2010-03-01T03:07:10Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-03-01T02:46:48Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-03-01T02:21:58Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-03-01T02:09:12Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-03-01T00:21:20Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-03-01T00:06:34Z

Bogdan Stancu: /* '''Mechanism''' */

Phosphoglucoisomerase

2010-02-28T23:59:36Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-02-28T23:57:59Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-02-28T23:57:27Z

Bogdan Stancu: /* '''Structure''' */

Phosphoglucoisomerase

2010-02-28T23:40:38Z

Bogdan Stancu: /* '''Structure''' */

File:Align.jpg

2010-02-28T23:32:56Z

Bogdan Stancu: Phosphoglucoisomerase multiple alignment

== Summary ==
Phosphoglucoisomerase multiple alignment
== Licensing ==
{{self|cc-by-3.0}}

Phosphoglucoisomerase

2010-02-28T22:58:40Z

Bogdan Stancu: /* '''Structure''' */

File:1iat.mmol

2010-02-28T22:53:33Z

Bogdan Stancu: Phosphoglucoisomerase dimer

Phosphoglucoisomerase dimer

Phosphoglucoisomerase

2010-02-28T22:41:16Z

Bogdan Stancu:

Phosphoglucoisomerase

2010-02-28T22:34:35Z

Bogdan Stancu:

Phosphoglucoisomerase

2010-02-27T07:41:19Z

Bogdan Stancu:

Phosphoglucoisomerase

2010-02-27T07:31:06Z

Bogdan Stancu: /* '''Links''' */

Phosphoglucoisomerase

2010-02-27T07:26:46Z

Bogdan Stancu:

Phosphoglucoisomerase

2010-02-27T07:21:55Z

Bogdan Stancu: /* '''Mechanism''' */

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Phosphoglucoisomerase" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis.
* Maturation factor(MF)
* Myofibril-bound serine protese inhibitor (MBSPI)

=='''Structure'''==
{{STRUCTURE_1hox | PDB=1hox| SCENE= }}

=='''Mechanism'''==
[[Image:Mech.png]]

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

File:Mech.png

2010-02-27T07:20:33Z

Bogdan Stancu: glucose-6-phosphate < - > fructose 6-phosphate

== Summary ==
glucose-6-phosphate < - > fructose 6-phosphate
== Licensing ==
{{self|cc-by-sa-3.0}}

Phosphoglucoisomerase

2010-02-26T23:07:17Z

Bogdan Stancu:

<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Phosphoglucoisomerase" />

'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:
* Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin.
* Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis.
* Maturation factor(MF)
* Myofibril-bound serine protese inhibitor (MBSPI)

=='''Structure'''==
{{STRUCTURE_1hox | PDB=1hox| SCENE= }}

=='''Mechanism'''==

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-02-26T22:37:38Z

Bogdan Stancu:

Phosphoglucoisomerase

2010-02-26T15:32:36Z

Bogdan Stancu:

{{STRUCTURE_1hox | PDB=1hox| SCENE= }}
'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis.

=='''Structure'''==

=='''Mechanism'''==

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-02-26T15:21:00Z

Bogdan Stancu:

{{STRUCTURE_1hox | PDB=1hox| SCENE= }}
'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.expasy.org/cgi-bin/nicezyme.pl?5.3.1.9 EC 5.3.1.9]), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis.

=='''Structure'''==

=='''Mechanism'''==

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-02-26T15:13:57Z

Bogdan Stancu:

{{STRUCTURE_1hox | PDB=1hox| SCENE= }}
'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.expasy.org/cgi-bin/nicezyme.pl?5.3.1.9 EC 5.3.1.9]), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of [[glycolysis]].

=='''Structure'''==

=='''Mechanism'''==

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>

Phosphoglucoisomerase

2010-02-26T15:10:58Z

Bogdan Stancu:

{{STRUCTURE_1hox | PDB=1hox| SCENE= }}
'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ({{EC number|5.3.1.9}}), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of [[glycolysis]].

=='''Structure'''==

=='''Mechanism'''==

=='''Links'''==

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=[[1hox]]<ref>PMID:11425306</ref>)

-Crystal Structure of human phosphoglucose isomerase (PDB=[[1iat]]<ref>PMID:11371164</ref>)

-Other available structures [[1dqr]], [[1g98]], [[1gzd]], [[1gzv]], [[1hm5]], [[1iri]], [[1jiq]], [[1jlh]], [[1koj]], [[1n8t]], [[1nuh]], [[1xtb]].

=='''References'''==
<references/>