Proteopedia - User contributions [en]

Sandbox Reserved 1094

2020-01-14T15:23:25Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>

KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),

KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

Optimum pH for its activity is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis of this enzyme induces catalytic activity loss: more than 200 mutations have been identified.
A mutation in a nucleotide in the sequence coding for G6PD leads to disruption of the normal expression of the enzyme, or to a disruption in the amino acid structure of the enzyme which leads to a loss or decrease of catalytic activity toward its substrate.

The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are a substitution of the bold amino acids by another one<ref>PMID: 11106479</ref>:

MVSEIKTLVT FFGG '''T''' GDLAK R '''K''' LYPSVFNL YKKGYLQKHF AIVGTA '''R''' '''Q''' AL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEK '''P''' FGTSYDTAAE LQNDLENAFD DNQLFRI '''D''' '''H''' '''Y''' LG '''K''' EMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN '''H''' TMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAA '''K''' QTRVDI VFKAGTFNFG SEQEAQEAVL SIII '''D''' PKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEP '''Y''' ERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG.

This sequence being the normal protein sequence found in L. ''mesenteroides''.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:22:45Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

Optimum pH for its activity is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis of this enzyme induces catalytic activity loss: more than 200 mutations have been identified.
A mutation in a nucleotide in the sequence coding for G6PD leads to disruption of the normal expression of the enzyme, or to a disruption in the amino acid structure of the enzyme which leads to a loss or decrease of catalytic activity toward its substrate.

The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are a substitution of the bold amino acids by another one<ref>PMID: 11106479</ref>:

MVSEIKTLVT FFGG '''T''' GDLAK R '''K''' LYPSVFNL YKKGYLQKHF AIVGTA '''R''' '''Q''' AL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEK '''P''' FGTSYDTAAE LQNDLENAFD DNQLFRI '''D''' '''H''' '''Y''' LG '''K''' EMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN '''H''' TMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAA '''K''' QTRVDI VFKAGTFNFG SEQEAQEAVL SIII '''D''' PKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEP '''Y''' ERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG.

This sequence being the normal protein sequence found in L. ''mesenteroides''.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:21:10Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

Optimum pH for its activity is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis of this enzyme induces catalytic activity loss: more than 200 mutations have been identified.
A mutation in a nucleotide in the sequence coding for G6PD leads to disruption of the normal expression of the enzyme, or to a disruption in the amino acid structure of the enzyme which leads to a loss or decrease of catalytic activity toward its substrate.

The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are a substitution of the bold amino acids by another one<ref>PMID: 11106479</ref>:

MVSEIKTLVT FFGG'''T'''GDLAK R'''K'''LYPSVFNL YKKGYLQKHF AIVGTA'''R''''''Q'''AL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEK'''P''' FGTSYDTAAE LQNDLENAFD DNQLFRI'''D''''''H''''''Y''' LG'''K'''EMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN '''H'''TMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAA'''K'''QTRVDI VFKAGTFNFG SEQEAQEAVL SIII'''D'''PKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEP'''Y'''ERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG.

This sequence being the normal protein sequence found in L. ''mesenteroides''.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:15:15Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

Optimum pH for its activity is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis of this enzyme induces catalytic activity loss: more than 200 mutations have been identified.
A mutation in a nucleotide in the sequence coding for G6PD leads to disruption of the normal expression of the enzyme, or to a disruption in the amino acid structure of the enzyme which leads to a loss or decrease of catalytic activity toward its substrate.

The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are<ref>PMID: 11106479</ref>:

MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG.

This sequence being the normal protein sequence found in L. ''mesenteroides''.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:04:02Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

Optimum pH for its activity is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:03:26Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:03:09Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T15:02:44Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc ''mesenteroides'' is a Bacilli Gram-positive bacterium that expresses this enzyme.
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides)<ref>GeneID:29577449</ref>.

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>
== References ==
<references/>

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:57:16Z

Loana Prost:

Sandbox Reserved 1094

2020-01-14T14:57:00Z

Loana Prost:

Sandbox Reserved 1094

2020-01-14T14:56:04Z

Loana Prost:

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2020-01-14T14:54:59Z

Loana Prost:

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2020-01-14T14:52:25Z

Loana Prost:

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Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:49:58Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:48:22Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH<ref>PMID: 9485426</ref>
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:46:52Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:45:55Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species <ref>PMID: 20608171</ref>.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:44:22Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc ''mesenteroides''==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:43:52Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:42:30Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-14T14:41:34Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1dpg' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene>
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-08T15:47:46Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD.

Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-08T15:35:39Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-08T15:35:14Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

</StructureSection>
== Proteopedia page contributors and editors ==
DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094

2020-01-08T15:32:35Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction as it produces a co-factor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:16:17Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.

4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:13:50Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:12:44Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

</StructureSection>
== References ==
<references/>
Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:11:02Z

Loana Prost: Undo revision 3142329 by Loana Prost (Talk)

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>
Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:10:35Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

</StructureSection>
== References ==
<references/>
Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:08:36Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>
Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.

Sandbox Reserved 1094

2020-01-08T15:06:10Z

Loana Prost:

{{Sandbox_ESBS_2019}}
==Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==
It is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway).
It also has a role in protecting cells from destruction because it produces a cofactor NADPH which plays a role in protecting cells from reactive oxygen species.

== Genomic context ==
It is coded by the G6PD gene (1461 nucleotides).

== Catalytic activity ==
D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH
KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD),
KM=8.0 µM for NADP, KM=160 µM for NAD
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway.

== Optimal activity conditions ==
Optimum pH is 5.4 - 8.9.

== Evolutionary conservation ==
We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary.

[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dpg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">

== Mutations ==
Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal
structure/function/reduce the expression of enzymes.

== Structural highlights ==
It is formed of a homodimer (dimer of two identical monomers).
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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== References ==
<references/>

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