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show all sequences of 1.1.1.94

Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism

Yeh, J.I.; Chinte, U.; Du, S.; Proc. Natl. Acad. Sci. USA 105, 3280-3285 (2008)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystal structure analysis: GlpD comprises two major domains, a soluble extramembraneous C-terminal cap domain (residues 389-501) and a N-terminal FAD-binding region, consisting of the substrate binding and base regions (residues 1-388). The dimeric enzyme is formed by monomers related by a noncrystallographic 2fold axis of symmetry and the dimer comprises the unique asymmetric unit. Electrostatic surface calculations show distinct regions of highly positive patches, located at the base region of the enzyme. These regions are likely involved with the negatively charged membrane phospholipid head groups. The cap domain, at the opposite side, exhibits highly negatively electrostatic potential, with large hydrophobic patches between these two distal regions of the enzyme, forming membrane interaction and proposed UQ-binding surfaces; structure of the native enzyme and in complex with dihydroxyacetone phosphate (2.1 A) and in separate complexes with substrate analogues, glyceraldehyde-3-phosphate (2.9 A), glyceric acid 2-phosphate (2.3 A), and phosphoenolpyruvate (2.1 A) are determined. Additionally, in complex with ubiquinone analogues, menadione (2.6 A) and 2-n-heptyl-4-hydroxyquinoline N-oxide (2.9 A)
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
glyceraldehyde-3-phosphate
competitive inhibitor
Escherichia coli
glyceric acid 2-phosphate
competitive inhibitor
Escherichia coli
phosphoenolpyruvate
competitive inhibitor
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P13035
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyceraldehyde-3-phosphate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
glyceric acid 2-phosphate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
phosphoenolpyruvate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
sn-glycerol 3-phosphate + NAD(P)+
-
689802
Escherichia coli
glycerone phosphate + NAD(P)H + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
crystal structure
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis: GlpD comprises two major domains, a soluble extramembraneous C-terminal cap domain (residues 389-501) and a N-terminal FAD-binding region, consisting of the substrate binding and base regions (residues 1-388). The dimeric enzyme is formed by monomers related by a noncrystallographic 2fold axis of symmetry and the dimer comprises the unique asymmetric unit. Electrostatic surface calculations show distinct regions of highly positive patches, located at the base region of the enzyme. These regions are likely involved with the negatively charged membrane phospholipid head groups. The cap domain, at the opposite side, exhibits highly negatively electrostatic potential, with large hydrophobic patches between these two distal regions of the enzyme, forming membrane interaction and proposed UQ-binding surfaces; structure of the native enzyme and in complex with dihydroxyacetone phosphate (2.1 A) and in separate complexes with substrate analogues, glyceraldehyde-3-phosphate (2.9 A), glyceric acid 2-phosphate (2.3 A), and phosphoenolpyruvate (2.1 A) are determined. Additionally, in complex with ubiquinone analogues, menadione (2.6 A) and 2-n-heptyl-4-hydroxyquinoline N-oxide (2.9 A)
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
glyceraldehyde-3-phosphate
competitive inhibitor
Escherichia coli
glyceric acid 2-phosphate
competitive inhibitor
Escherichia coli
phosphoenolpyruvate
competitive inhibitor
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
glyceraldehyde-3-phosphate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
glyceric acid 2-phosphate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
phosphoenolpyruvate + NAD(P)+
crystal structure with complexed substrate analogue is determined
689802
Escherichia coli
?
-
-
-
?
sn-glycerol 3-phosphate + NAD(P)+
-
689802
Escherichia coli
glycerone phosphate + NAD(P)H + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
crystal structure
Escherichia coli
Other publictions for EC 1.1.1.94
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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689802
Yeh
Structure of glycerol-3-phosph ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
105
3280-3285
2008
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J. Biol. Chem.
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1980
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Escherichia coli
J. Biol. Chem.
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1978
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