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Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+] and Organism(s) Escherichia coli and UniProt Accession P13035

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IUBMB Comments
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
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This record set is specific for:
Escherichia coli
UNIPROT: P13035
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
sn-glycerol-3-phosphate dehydrogenase, cvgpd1, nadp-dependent glycerol-3-phosphate dehydrogenase, rp442, nad(p)h-dependent glycerol-3-phosphate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycerol 3-phosphate dehydrogenase (NADP)
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glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate))
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L-glycerol-3-phosphate:NAD(P) oxidoreductase
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NAD(P)H-dependent dihydroxyacetone-phosphate reductase
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NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
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NADP-dependent glycerol-3-phosphate dehydrogenase
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sn-glycerol-3-phosphate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
show the reaction diagram
bimolecular kinetic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-30-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
show the reaction diagram
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
show the reaction diagram
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
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-
-
-
?
glycerone phosphate + reduced nicotinamide hypoxanthine dinucleotide
sn-glycerol-3-phosphate + oxidized nicotinamide hypoxanthine dinucleotide
show the reaction diagram
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-
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?
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
show the reaction diagram
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r
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
show the reaction diagram
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-
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
show the reaction diagram
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-
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r
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
show the reaction diagram
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enzyme regulation, overview
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r
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
show the reaction diagram
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r
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deamino-NAD+
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2fold activity compared to NAD+
NADP+
NADPH
nicotinamide hypoxanthine dinucleotide
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-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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100 mM, 68% inhibition, 10 mM, 8% inhibition
2',5'-ADP
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3,4-dihydroxybutyl 1-phosphonate
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competitive versus dihydroxyacetone phosphate, binding to a regulatory site
ADP-ribose
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dihydroxyacetone phosphate
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noncompetitive versus NADP+
DL-glycerol 3-phosphate
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0.05 mM, 26% inhibition
ethylene glycol phosphate
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binding to the active 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
K2PO4-
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100 mM, 95% inhibition, 10 mM, 27% inhibition
K2SO4
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100 mM, 60% inhibition
KCl
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100 mM, 47% inhibition
Na2PO4-
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100 mM, 92% inhibition, 10 mM, 27% inhibition
Na2SO4
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100 mM, 63% inhibition
NaCl
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100 mM, 47% inhibition
NADP+
NADPH
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competitive versus NADP+
NH4Cl
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100 mM, 37% inhibition
palmitoyl-CoA
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0.0015 mM, 52% inhibition
sn-glycerol-3-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
glycerol-3-phosphate
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0.17
glycerone phosphate
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0.004 - 0.0045
NADH
0.0037 - 0.01
NADPH
0.005
reduced nicotinamide hypoxanthine dinucleotide
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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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 2
2',5'-ADP
0.7 - 0.8
ADP
0.1 - 0.21
ADP-ribose
4.8 - 5
AMP
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
0.2 - 0.22
NAD+
0.19 - 0.25
NADP+
10
NMN
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pH 7.4, 23°C, wild-type enzyme and feedback-resistant mutant enzyme
0.0044 - 0.043
sn-glycerol-3-phosphate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
streptomycin, ammonium sulfate, DEAE-Sephadex, Sephadex G-150, DEAE-Sephadex
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
synthesis
development of a whole-cell biocatalyst for NAD(P)H cofactor regeneration that employs permeabilized Escherichia coli cells in which the glpD and gldA genes are deleted and the gpsA gene is overexpressed. The biocatalyst involves an economical substrate, bifunctional regeneration of NAD(P)H, and simple reaction conditions as well as a stable environment for enzymes, and is applicable to a variety of oxidoreductase reactions requiring NAD(P)H regeneration
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Rho, H.; Choi, K.
Cofactor regeneration using permeabilized Escherichia coli expressing NAD(P)+-dependent glycerol-3-phosphate dehydrogenase
J. Microbiol. Biotechnol.
28
1346-1351
2018
Escherichia coli (P0A6S7)
Manually annotated by BRENDA team