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Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+] for references in articles please use BRENDA:EC1.1.1.94Word Map on EC 1.1.1.94
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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glycerol-3-phosphate dehydrogenase [NAD(P)+]
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sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
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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CDP-diacylglycerol biosynthesis I
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CDP-diacylglycerol biosynthesis II
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CDP-diacylglycerol biosynthesis III
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glucosylglycerol biosynthesis
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CDP-diacylglycerol biosynthesis
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Glycerophospholipid metabolism
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Biosynthesis of secondary metabolites
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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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glycerol 3-phosphate dehydrogenase
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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
GpsA
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sn-glycerol-3-phosphate dehydrogenase
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sn-glycerol-3-phosphate dehydrogenase
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sn-glycerol-3-phosphate dehydrogenase
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and strain BB26-36-R2
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UniProt
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UniProt
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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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glyceraldehyde-3-phosphate + NAD(P)+
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crystal structure with complexed substrate analogue is determined
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glyceric acid 2-phosphate + NAD(P)+
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crystal structure with complexed substrate analogue is determined
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glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
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)+
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crystal structure with complexed substrate analogue is determined
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sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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r
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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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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glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
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glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
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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 + 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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sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
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r
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glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
sn-glycerol 3-phosphate + NAD(P)+
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enzyme regulation, overview
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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 + NADP+
glycerone phosphate + NADPH + H+
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glycerone phosphate + NAD(P)H
sn-glycerol-3-phosphate + NAD(P)+
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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
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deamino-NAD+
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2fold activity compared to NAD+
nicotinamide hypoxanthine dinucleotide
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NAD+
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NADH
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NADH
NADPH is preferred over NADH as the cofactor
NADP+
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2fold activity compared to NAD+
NADP+
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B-type specificity of wild-type and feedback-resistant mutant enzyme
NADPH
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NADPH
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B-type specificity of wild-type and feedback-resistant mutant enzyme
NADPH
NADPH is preferred over NADH as the cofactor
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(NH4)2SO4
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100 mM, 68% inhibition, 10 mM, 8% inhibition
3,4-dihydroxybutyl 1-phosphonate
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competitive versus dihydroxyacetone phosphate, binding to a regulatory site
adenosine
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competitive vs. NAD+
Adenosine diphosphate
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competitive vs. NAD+
adenosine diphosphoribose
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competitive vs. NAD+
adenylic acid
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competitive vs. NAD+
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
glyceraldehyde-3-phosphate
competitive inhibitor
glyceric acid 2-phosphate
competitive inhibitor
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
N1-butylnicotinamide chloride
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competitive vs. NAD+
N1-decylnicotinamide chloride
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competitive vs. NAD+
N1-dodecylnicotinamide chloride
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competitive vs. NAD+
N1-ethylnicotinamide chloride
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competitive vs. NAD+
N1-heptylnicotinamide chloride
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competitive vs. NAD+
N1-hexylnicotinamide chloride
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competitive vs. NAD+
N1-methylnicotinamide chloride
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competitive vs. NAD+
N1-nonylnicotinamide chloride
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competitive vs. NAD+
N1-octylnicotinamide chloride
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competitive vs. NAD+
N1-pentylnicotinamide chloride
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competitive vs. NAD+
N1-propylnicotinamide chloride
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competitive vs. NAD+
N1-undecylnicotinamide chloride
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competitive vs. NAD+
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
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
phosphoenolpyruvate
competitive inhibitor
NADP+
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competitive versus 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
sn-glycerol-3-phosphate
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the wild-type enzyme is feedback inhibited
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0.21
glycerol-3-phosphate
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0.17 - 0.528
glycerone phosphate
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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0.17
glycerone phosphate
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0.528
glycerone phosphate
cosubstrate NADPH, pH 7.4, temperature not specified in the publication
0.004
NADH
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.0045
NADH
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pH 7.4, 23°C, wild-type mutant enzyme
0.0037
NADPH
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.0041
NADPH
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pH 7.4, 23°C, wild-type mutant enzyme
0.048
NADPH
pH 7.4, temperature not specified in the publication
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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
0.0044 - 0.043
sn-glycerol-3-phosphate
additional information
additional information
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1.8
2',5'-ADP
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pH 7.4, 23°C, wild-type enzyme
2
2',5'-ADP
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.7
ADP
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.8
ADP
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pH 7.4, 23°C, wild-type enzyme
0.1
ADP-ribose
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pH 7.4, 23°C, wild-type enzyme
0.21
ADP-ribose
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pH 7.4, 23°C, feedback-resistant mutant enzyme
4.8
AMP
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pH 7.4, 23°C, feedback-resistant mutant enzyme
5
AMP
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pH 7.4, 23°C, wild-type enzyme
0.2
NAD+
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pH 7.4, 23°C, wild-type enzyme
0.22
NAD+
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.19
NADP+
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pH 7.4, 23°C, feedback-resistant mutant enzyme
0.25
NADP+
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pH 7.4, 23°C, wild-type enzyme
0.0044
sn-glycerol-3-phosphate
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pH 7.4, 23°C, wild-type enzyme
0.043
sn-glycerol-3-phosphate
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pH 7.4, 23°C, resistant mutant enzyme
additional information
additional information
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inhibition kinetics
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additional information
additional information
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product inhibition kinetics
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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
70
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purified wild-type enzyme
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7.4
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23
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assay at
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brenda
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O29390
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126);
Q83BJ0
Coxiella burnetii (strain RSA 493 / Nine Mile phase I);
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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
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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
36600
x * 36600, SDS-PAGE and calculated for His-tagged protein
48300
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feedback inhibition-resistant mutant, sedimentation equilibrium analysis
49000
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wild-type enzyme, gel filtration
50000
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feedback inhibition-resistant mutant, gel filtration
50700
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wild-type enzyme, sedimentation equilibrium analysis
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?
x * 36600, SDS-PAGE and calculated for His-tagged protein
dimer
crystal structure
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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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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-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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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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expression in Escherichia coli
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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
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heterologous expression in Escherichia coli complements an Escherichia coli gpsA mutant
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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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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, Escherichia coli (P13035)
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
Candida 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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