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Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+]
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1.1.1.94 glycerol-3-phosphate dehydrogenase [NAD(P)+]IUBMB Comments
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
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Word Map
- 1.1.1.94
- drosophila
- melanogaster
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1.1.1.8
-
stromal-vascular
-
bergmann
-
allozyme
-
glycerol-p
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
CvGPD1, G3PD, G3PDH, GLPD, glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate dehydrogenase (NADP), glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)), GPDH, GpsA, L-glycerol-3-phosphate:NAD(P) oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycerol 3-phosphate dehydrogenase (NADP)
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-
-
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glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate))
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-
-
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GpsA
L-glycerol-3-phosphate:NAD(P) oxidoreductase
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-
-
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NAD(P)H-dependent dihydroxyacetone-phosphate reductase
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-
-
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NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
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-
-
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sn-glycerol-3-phosphate dehydrogenase
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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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-
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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
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-
-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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
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-
?
glycerone phosphate + NADPH + H+
sn-glycerol 3-phosphate + NADP+
favoured reaction direction
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-
r
glycerone phosphate + reduced nicotinamide hypoxanthine dinucleotide
sn-glycerol-3-phosphate + oxidized nicotinamide hypoxanthine dinucleotide
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-
-
-
?
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
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r
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
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enzyme regulation, overview
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-
r
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
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-
-
r
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
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-
-
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+
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-
-
-
?
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
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-
-
r
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NATURAL SUBSTRATE
NATURAL 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
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)+
-
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
-
B-type specificity of wild-type and feedback-resistant mutant enzyme
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INHIBITOR
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
-
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
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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
-
during growth on wheat dough at water activity at the time of harvest 0.98
0.012
-
during growth on wheat dough at water activity at the time of harvest 0.96
0.014
-
during growth on wheat grains at water activity at the time of harvest 0.97
0.028
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
-
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
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feedback inhibition-resistant mutant, sedimentation equilibrium analysis
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SUBUNIT
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
existence of a naturally occurring feedback inhibition-resistant mutant
additional information
-
existence of a naturally occurring feedback inhibition-resistant mutant
additional information
-
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
additional information
-
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
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kito, M.; Pizer, L.I.
Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli
J. Biol. Chem.
244
3316-3323
1969
Escherichia coli
brenda
Kim, S.J.; anderson, B.M.
Properties of the nicotinamide adenine dinucleotide-binding sites of L-alpha-glycerolphosphate dehydrogenase
J. Biol. Chem.
243
3351-3356
1968
Oryctolagus cuniculus
brenda
Ruijter, G.J.G.; Visser, J.; Rinzema, A.
Polyol accumulation by Aspergillus oryzae at low water activity in solid-state fermentation
Microbiology
150
1095-1101
2004
Aspergillus oryzae
brenda
Edgar, J.R.; Bell, R.M.
Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Purification and physical characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase
J. Biol. Chem.
253
6348-6353
1978
Escherichia coli K-12
brenda
Edgar, J.R.; Bell, R.M.
Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase
J. Biol. Chem.
253
6354-6363
1978
Escherichia coli
brenda
Edgar, J.R.; Bell, R.M.
Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase
J. Biol. Chem.
255
3492-3497
1980
Escherichia coli
brenda
Yeh, J.I.; Chinte, U.; Du, S.
Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
Proc. Natl. Acad. Sci. USA
105
3280-3285
2008
Escherichia coli (P13035), Escherichia coli
brenda
Watanabe, Y.; Nagayama, K.; Tamai, Y.
Expression of glycerol 3-phosphate dehydrogenase gene (CvGPD1) in salt-tolerant yeast Candida versatilis is stimulated by high concentrations of NaCl
Yeast
25
107-116
2008
Wickerhamiella versatilis
brenda
Frohlich, K.M.; Roberts, R.A.; Housley, N.A.; Audia, J.P.
Rickettsia prowazekii uses an sn-glycerol-3-phosphate dehydrogenase and a novel dihydroxyacetone phosphate transport system to supply triose phosphate for phospholipid biosynthesis
J. Bacteriol.
192
4281-4288
2010
Rickettsia prowazekii (Q9ZDA0), Rickettsia prowazekii
brenda
Shen, W.; Li, J.Q.; Dauk, M.; Huang, Y.; Periappuram, C.; Wei, Y.; Zou, J.
Metabolic and transcriptional responses of glycerolipid pathways to a perturbation of glycerol 3-phosphate metabolism in Arabidopsis
J. Biol. Chem.
285
22957-22965
2010
Escherichia coli
brenda
Lakshmanan, M.; Yu, K.; Koduru, L.; Lee, D.Y.
In silico model-driven cofactor engineering strategies for improving the overall NADP(H) turnover in microbial cell factories
J. Ind. Microbiol. Biotechnol.
42
1401-1414
2015
Escherichia coli
brenda
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