Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.94
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RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase [NAD(P)+]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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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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Glycerophospholipid metabolism
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CDP-diacylglycerol biosynthesis
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
and strain BB26-36-R2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glyceraldehyde-3-phosphate + NAD(P)+
?
show the reaction diagram
crystal structure with complexed substrate analogue is determined
-
-
?
glyceric acid 2-phosphate + NAD(P)+
?
show the reaction diagram
crystal structure with complexed substrate analogue is determined
-
-
?
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
glycerone phosphate + NADPH + H+
sn-glycerol 3-phosphate + NADP+
show the reaction diagram
favoured reaction direction
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r
glycerone phosphate + reduced nicotinamide hypoxanthine dinucleotide
sn-glycerol-3-phosphate + oxidized nicotinamide hypoxanthine dinucleotide
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + NAD(P)+
?
show the reaction diagram
crystal structure with complexed substrate analogue is determined
-
-
?
sn-glycerol 3-phosphate + NAD(P)+
glycerone phosphate + NAD(P)H + H+
show the reaction diagram
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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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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-
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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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-
INHIBITORS
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
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+
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
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
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
phosphoenolpyruvate
competitive inhibitor
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 - 0.528
glycerone phosphate
0.004 - 0.0045
NADH
0.0037 - 0.048
NADPH
0.005
reduced nicotinamide hypoxanthine dinucleotide
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pH 7.4, 23C, 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, 23C, wild-type enzyme and feedback-resistant mutant enzyme
1.4
ethylene glycol phosphate
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pH 7.4, 23C, 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, 23C, 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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
-
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36600, SDS-PAGE and calculated for His-tagged protein
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)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 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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recombinant protein
streptomycin, ammonium sulfate, DEAE-Sephadex, Sephadex G-150, DEAE-Sephadex
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
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