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Enzyme Nomenclature
Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.94
Word Map on EC 1.1.1.94
- 1.1.1.94
- melanogaster
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1.1.1.8
-
stromal-vascular
-
glycerol-p
-
bergmann
-
allozyme
- agriculture
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.94
-
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RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
-
-
-
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sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
bimolecular kinetic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
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CAS REGISTRY NUMBER
COMMENTARY
37250-30-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Rickettsia prowazekii is unable to synthesize glycerone phosphate as a substrate for the GpsA enzymatic reaction. Purified Rickettsia prowazekii transports and incorporates glycerone phosphate into phospholipids, implicating a role for GpsA in vivo as part of a rickettsial G3P acquisition pathway for phospholipid biosynthesis
physiological function
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in transgenic Arabidopsis thaliana lines with a feedback-resistant glycerol-3-phosphate dehydrogenase gene from Escherichia coli, feedback-resistant glycerol-3-phosphate dehydrogenase is detected in the cytosol, but augmented glycerol-3-phosphate levels are observed in the cytosol as well as in chloroplasts. Glycerolipid composition and fatty acid positional distribution analyses reveal an altered fatty acid flux that affects not only the molar ratios of glycerolipid species but also their fatty acid composition. Changes in glycerol-3-phosphate metabolism cause altered expression of a broad array of genes. Transcript levels of the enzymes involved in the prokaryotic pathway are mostly induced, whereas genes of the eukaryotic pathway enzymes are largely suppressed
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glyceraldehyde-3-phosphate + NAD(P)+
?
crystal structure with complexed substrate analogue is determined
-
-
?
glyceric acid 2-phosphate + NAD(P)+
?
crystal structure with complexed substrate analogue is determined
-
-
?
glycerone phosphate + NADPH + H+
sn-glycerol 3-phosphate + NADP+
favoured reaction direction
-
-
r
glycerone phosphate + reduced nicotinamide hypoxanthine dinucleotide
sn-glycerol-3-phosphate + oxidized nicotinamide hypoxanthine dinucleotide
-
-
-
-
?
phosphoenolpyruvate + NAD(P)+
?
crystal structure with complexed substrate analogue is determined
-
-
?
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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i.e. dihydroxyacetone phosphate
product analysis
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r
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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i.e. dihydroxyacetone phosphate
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-
r
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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the enzyme is required for biosynthesis of sn-glycerol-3-phosphate, overview
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-
r
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
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i.e. dihydroxyacetone phosphate
-
-
r
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
-
enzyme regulation, overview
-
-
r
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
r
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
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-
-
-
?
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
-
-
-
?
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
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-
-
r
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
-
enzyme regulation, overview
-
-
r
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
-
-
-
r
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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the enzyme is required for biosynthesis of sn-glycerol-3-phosphate, overview
-
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
B-type specificity of wild-type and feedback-resistant mutant enzyme
NADPH
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B-type specificity of wild-type and feedback-resistant mutant enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-dihydroxybutyl 1-phosphonate
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competitive versus dihydroxyacetone phosphate, binding to a regulatory site
glycerol 3-phosphate
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50% inhibition with 0.035 mM, sigmoid inhibition curve, competitive inhibition vs. glycerone phosphate, uncompetitive vs. NADPH
sn-glycerol-3-phosphate
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product inhibition at an allosteric, regulatory site, competitive versus dihydroxyacetone phosphate, noncompetitive versus NADPH, the wild-type enzyme is feedback inhibited
sn-glycerol-3-phosphate
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the wild-type enzyme is feedback regulated, competitive versus dihydroxyacetone phosphate, binding to a regulatory site
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
reduced nicotinamide hypoxanthine dinucleotide
-
pH 7.4, 23°C, wild-type mutant enzyme and feedback-resistant mutant enzyme
additional information
additional information
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kinetics and bimolecular kinetic mechanism
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0.528
glycerone phosphate
cosubstrate NADPH, pH 7.4, temperature not specified in the publication
0.048
NADPH
pH 7.4, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
ATP
-
pH 7.4, 23°C, wild-type enzyme and feedback-resistant mutant enzyme
1.4
ethylene glycol phosphate
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pH 7.4, 23°C, wild-type and feedback-resistant mutant enzyme
10
NMN
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pH 7.4, 23°C, wild-type enzyme and feedback-resistant mutant enzyme
additional information
additional information
-
product inhibition kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.011
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during growth on wheat dough at water activity at the time of harvest 0.98
0.012
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during growth on wheat dough at water activity at the time of harvest 0.96
0.014
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during growth on wheat grains at water activity at the time of harvest 0.97
0.028
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during growth on wheat grains at water activity at the time of harvest 1.00
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25900
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2 * 32500, native wild-type enzyme, SDS-PAGE, 2 * 25900, wild-type enzyme, denaturing sedimentation equilibrium analysis, 2 * 26000, feedback inhibition-resistant mutant, sedimentation equilibrium analysis
26000
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2 * 32500, native wild-type enzyme, SDS-PAGE, 2 * 25900, wild-type enzyme, denaturing sedimentation equilibrium analysis, 2 * 26000, feedback inhibition-resistant mutant, sedimentation equilibrium analysis
32500
-
2 * 32500, native wild-type enzyme, SDS-PAGE, 2 * 25900, wild-type enzyme, denaturing sedimentation equilibrium analysis, 2 * 26000, feedback inhibition-resistant mutant, sedimentation equilibrium analysis
48300
-
feedback inhibition-resistant mutant, sedimentation equilibrium analysis
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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2 * 32500, native wild-type enzyme, SDS-PAGE, 2 * 25900, wild-type enzyme, denaturing sedimentation equilibrium analysis, 2 * 26000, feedback inhibition-resistant mutant, sedimentation equilibrium analysis
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified concentrated wild-type enzyme, 50% glycerol, 25 mM Tris-HCl, pH 7.4, 0.5 mM DTT, 0.2 M NaCl, 5 mM glycerol-3-phosphate, 1 month, over 90% remaining activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native wild-type enzyme from Escherichia coli K12 12000fold by streptomycin and ammonum sulfate fractionation, adsorption, hydroxy apatite, and anion exchange chromatography, and gel filtration to over 95% purity, feedback inhibition-resistant mutant from strain BB26-36-R2
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streptomycin, ammonium sulfate, DEAE-Sephadex, Sephadex G-150, DEAE-Sephadex
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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glycerol 3-phosphate dehydrogenase gene (CvGPD1) from salt-tolerant yeast Candida versatilisis is expressed in glycerol synthesis-deficient Saccharomyces cerevisiae cells, the salt tolerance of the recombinant strain is enhanced, and NADP+-dependent GPDH, Cvgpd1p synthesis and recovery of glycerol synthesis are confirmed. The transcription of CvGPD1 in Candida versatilis cells is stimulated by high concentrations of NaCl
additional information
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existence of a naturally occurring feedback inhibition-resistant mutant
additional information
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existence of a naturally occurring feedback inhibition-resistant mutant in strain BB26-36-R2
additional information
heterologous expression in Escherichia coli complements an Escherichia coli gpsA mutant
additional information
-
heterologous expression in Escherichia coli complements an Escherichia coli gpsA mutant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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in transgenic Arabidopsis thaliana lines with a feedback-resistant glycerol-3-phosphate dehydrogenase gene from Escherichia coli, feedback-resistant glycerol-3-phosphate dehydrogenase is detected in the cytosol, but augmented glycerol-3-phosphate levels are observed in the cytosol as well as in chloroplasts. Glycerolipid composition and fatty acid positional distribution analyses reveal an altered fatty acid flux that affects not only the molar ratios of glycerolipid species but also their fatty acid composition. Changes in glycerol-3-phosphate metabolism cause altered expression of a broad array of genes. Transcript levels of the enzymes involved in the prokaryotic pathway are mostly induced, whereas genes of the eukaryotic pathway enzymes are largely suppressed
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