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Enzyme Nomenclature
Information on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.8
Word Map on EC 1.1.1.8
- 1.1.1.8
- adipose
- adipocytes
- glyceraldehyde-3-phosphate
-
glycolytic
-
preadipocytes
- glyceraldehyde
-
malic
-
adipogenesis
-
adipogenic
- dhap
-
omental
-
allozyme
-
alpha-gpdh
-
perirenal
-
3-phosphatase
-
fad-linked
-
1.2.1.12
- synthesis
- food industry
- biotechnology
- nutrition
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.8
-
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RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
ordered bi-bi mechanism
-
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
-
-
-
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
one active site per enzyme molecule
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
one active site per enzyme molecule
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
one active site per enzyme molecule
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
equilibrium random-bi-bi reaction mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
ordered ternary-complex mechanism, NADH binds first
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
equilibrium random-bi-bi reaction mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
ordered bi-bi mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
equilibrium random-bi-bi reaction mechanism
-
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
equilibrium random-bi-bi reaction mechanism
-
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
-
-
-
-
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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+ 2-oxidoreductase
Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
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CAS REGISTRY NUMBER
COMMENTARY
9075-65-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; an osmotolerant yeast isolated from soil outside a food factory
UniProt
; an osmotolerant yeast isolated from soil outside a food factory
UniProt
-
-
-
inbred Lewis strain euthyroid, hyperthyroid and hypothyroid male and female rats
-
-
overexprssion of glycerol-3-phosphate dehydrogenase results in the production of more glycerol and less ethanol during fermentation
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases, overview
evolution
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval; the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval
evolution
Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7%
evolution
Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7%
evolution
-
the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval; the intronless genes Cagpd1 and Cagpd2, encoding the two isozymes of the organism, are both predicted to encode a 378 amino acid polypeptide, and the deduced amino acid sequences mutually show 76% identity. Genes Cagpd1 and Cagpd2 are located tandemly in a locus of genomic DNA within a 262 bp interval
-
malfunction
-
mutation N270A results in a 7.7 kcal/mol decrease in the intrinsic phosphodianion binding energy, which is larger than the 5.6 kcal/mol effect of the mutation on the stability of the transition state for reduction of DHAP. A 2.2 kcal/mol stabilization of the transition state for unactivated hydride transfer to the truncated substrate glycolaldehyde, and a change in the effect of phosphite dianion on GPDH-catalyzed reduction of glycolaldehyde, from strongly activating to inhibiting. The N270A mutation breaks the network of hydrogen bonding side chains, Asn270, Thr264, Asn205, Lys204, Asp260, and Lys120, which connect the dianion activation and catalytic sites of GPDH. The disruption dramatically alters the performance of GPDH at these sites
metabolism
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism. Glycerol 3-phosphate from the breakdown of phospholipids and triglycerides (via glycerol kinase) is converted into the glycolysis intermediate dihydroxyacetone phosphate, while the reverse reaction produces glycerol 3-phosphate, which is required for the synthesis of triglycerides and phospholipids
metabolism
-
glycerol-3-phosphate dehydrogenase is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate to glycerol-3-phosphate
metabolism
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
the enzyme is a key enzyme in the glycerol biosynthesis pathway; the enzyme is a key enzyme in the glycerol biosynthesis pathway
metabolism
-
isoform G3PD1 plays an important role during fatty acid accumulation in Mortierelle alpine
metabolism
glycerol-3-phosphate dehydrogenase (G3PDH) is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate
metabolism
Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway
metabolism
Saccharomyces kudriavzevii has changed the metabolism to promote the branch of the glycolytic pathway involved in glycerol production to adapt to low temperature environments and maintain the NAD+/NADH ratio in alcoholic fermentations. Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway
metabolism
-
the enzyme is a key enzyme in the glycerol biosynthesis pathway; the enzyme is a key enzyme in the glycerol biosynthesis pathway
-
metabolism
-
glycerol-3-phosphate dehydrogenase is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate to glycerol-3-phosphate
-
metabolism
-
isoform G3PD1 plays an important role during fatty acid accumulation in Mortierelle alpine
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physiological function
-
no change in G3PDH activity is observed under salt stress of 0.5 M NaCl, while significant increase in G3PDH activity is observed at high salt concentration of 1.5 M NaCl. G3PDH activity is suppressed at all growth phases of the organism under temperature stress of 20°C and 40°C. No significant change in G3PDH activity is observed at mid log/stationary phase of growth under pH stress condition. At late stationary phase of growth, G3PDH activity increases with decrease in pH of the medium as compared to control
physiological function
-
GPDH-1 in the cytoplasm and a glycerophosphate oxidase in the mitochondrion cooperate in Drosophila flight muscles to generate the ATP needed for muscle contraction
physiological function
the cytosolic activity of glycerol-3-phosphate dehydrogenase 1 plays an important role in the synthesis of triacylglycerol and in the transport of reducing equivalents from the cytosol to mitochondria
physiological function
-
in spermatozoa from homozygous Gpd2 deletion mice, in the absence of Gpd2, hyperactivation and acrosome reaction are significantly altered, and a few changes in protein tyrosine phosphorylation are also observed during capacitation. GPD2 activity is required for generation of reactive oxygen species in mouse spermatozoa during capacitation, failing which, capacitation is impaired
physiological function
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The concerted action of cytosolic (NAD+-dependent) G3PDHs and membrane-bound (FAD-dependent) G3PDHs transfers reducing equivalents from cytosolic NADH into the electron-transport chain of both bacteria and mitochondria
physiological function
-
glycerol 3-phosphate dehydrogenase plays an important role in the energy metabolism and nutrition metabolism
physiological function
-
G3PDH is an important locus in fuel catabolism in hibernating species
physiological function
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
the enzyme is involved in osmotic stress response; the enzyme is involved in osmotic stress response; two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response; two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response
physiological function
-
isoform GPDH-1 is involved in flight metabolism; isoform GPDH-2 provides lipid precursors
physiological function
-
role for Asn270 in glycerol 3-phosphate dehydrogenase-catalyzed hydride transfer
physiological function
-
the hibernating form of G3PDH from the liver of Richardson's ground squirrels maintains better functionality at low temperatures and has greater temperature stability. These properties help sustain G3PDH function over the wide range of body temperatures experienced by the species as they cycle though torpor-arousal bouts over the hibernating season
physiological function
isoform GPDH2 is involved in glycerol synthesis and osmotic stress tolerance; isoform GPDH3 is involved in glycerol synthesis and osmotic stress tolerance
physiological function
the enzyme catalyzes the formation of glycerol 3-phosphate, the backbone of many membrane lipids. Overexpression of plastidic enzyme G3pDH enhances biosynthesis of plastid-localized lipids in rice, and photosynthetic efficiency is enhanced in the transgenic plants
physiological function
the glycerol-DHAP cycle pathway, which is driven by enzyme G3PDH, is considered as the rate-limiting enzyme to regulate the glycerol level under osmotic shocks
physiological function
glycerol is increased in Saccharomyces kudriavzevii mainly due to increased Vmax of the Gpd1p enzyme
physiological function
-
the enzyme is involved in osmotic stress response; the enzyme is involved in osmotic stress response; two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response; two glycerol 3-phosphate dehydrogenase isozymes from Candida versatilis SN-18 play an important role in glycerol biosynthesis under osmotic stress. The enzyme is involved in osmotic stress response
-
physiological function
-
no change in G3PDH activity is observed under salt stress of 0.5 M NaCl, while significant increase in G3PDH activity is observed at high salt concentration of 1.5 M NaCl. G3PDH activity is suppressed at all growth phases of the organism under temperature stress of 20°C and 40°C. No significant change in G3PDH activity is observed at mid log/stationary phase of growth under pH stress condition. At late stationary phase of growth, G3PDH activity increases with decrease in pH of the medium as compared to control
-
physiological function
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the enzyme is important for osmotolerance
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physiological function
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the cytosolic activity of glycerol-3-phosphate dehydrogenase 1 plays an important role in the synthesis of triacylglycerol and in the transport of reducing equivalents from the cytosol to mitochondria
-
additional information
-
when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
additional information
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structure-function analysis of wild-type and mutant enzymes, overview
additional information
-
three-dimensional structure modeling of enzyme G3PDH to identify the potential phosphorylation site (83Tyr) responsible for the differential phosphorylation between euthermic and hibernator G3PDH. Structural and functional changes in G3PDH support the enzyme's function at a low core body temperature experienced during the species hibernating season
additional information
-
when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
-
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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
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 1-phosphate + NAD+
-
-
-
r
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
an electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analysis
-
-
?
dihydroxyacetone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
r
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
?
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
mGPDH is involved in maintaining a high rate of glycolysis and is an important site of electron leakage leading to production of reactive oxygen species in prostate cancer cells
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
favoured reaction of heart isozyme II6.1
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
reverse reaction favoured direction
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
NAD+-linked cGPDH can interconvert DHAP and glycerol 3-phosphate
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
-
the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH
-
?
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
-
the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH
-
?
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme
-
-
?
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
-
the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH
-
?
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme
-
-
?
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
-
the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH
-
?
additional information
?
-
-
increased glycerol-3-phosphate levels are associated with enhanced resistance to Colletotrichum higginsianum. Overexpression of the host GLY1 gene, which encodes a G3P dehydrogenase, confers enhanced resistance to the hemibiotrophic fungus Colletotrichum higginsianum
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
glucose-6-phosphate, acetaldehyde, oxaloacetate
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
glucose-6-phosphate, acetaldehyde, oxaloacetate
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of DhGPD1 (glycerol 3-phosphate dehydrogenase) and DhGPP2 (glycerol 3-phosphatase)
-
-
-
additional information
?
-
-
involved in cellular acidosis, oxidoresistance, apoptosis by both acidosis and cell-cell contact inhibition, cell growth, and the generation of recombinant proteins
-
-
-
additional information
?
-
-
a decrease in temperature alone is sufficient to activate glycerol production and an increase in GPDH activity plays a critical role in the early stages of this process
-
-
-
additional information
?
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
DL-glyceraldehyde, phosphohydroxypyruvate
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate (G3P) at 37°C and 22°C, while at 5°C, there is a significant increase in affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 1-phosphate + NAD+
Q949Q0
-
-
-
r
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
Q52ZA0, V9MH41
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
Q52ZA0
-
-
-
r
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
Q949Q0
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
mGPDH is involved in maintaining a high rate of glycolysis and is an important site of electron leakage leading to production of reactive oxygen species in prostate cancer cells
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
favoured reaction of heart isozyme II6.1
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
reverse reaction favoured direction
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
-
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
Q949Q0
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A140JW76, A0A140JW77, A0A14OJW76, A0A14OJW77
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
Q52ZA0, V9MH41
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
P08507
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
Q00055
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
A0A060KZ16
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
r
additional information
?
-
-
increased glycerol-3-phosphate levels are associated with enhanced resistance to Colletotrichum higginsianum. Overexpression of the host GLY1 gene, which encodes a G3P dehydrogenase, confers enhanced resistance to the hemibiotrophic fungus Colletotrichum higginsianum
-
-
-
additional information
?
-
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of DhGPD1 (glycerol 3-phosphate dehydrogenase) and DhGPP2 (glycerol 3-phosphatase)
-
-
-
additional information
?
-
-
involved in cellular acidosis, oxidoresistance, apoptosis by both acidosis and cell-cell contact inhibition, cell growth, and the generation of recombinant proteins
-
-
-
additional information
?
-
-
a decrease in temperature alone is sufficient to activate glycerol production and an increase in GPDH activity plays a critical role in the early stages of this process
-
-
-
additional information
?
-
Q00055
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
-
additional information
?
-
-
relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate (G3P) at 37°C and 22°C, while at 5°C, there is a significant increase in affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
isozyme GPDH1 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme; isozyme GPDH1 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme; isozyme GPDH2 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme; isozyme GPDH2 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme
additional information
-
3-acetylpyridine-NAD+ 1.5% as effective as NAD+; deamino-NAD+ 68% as effective as NAD+
-
additional information
-
activity with dihydroxyacetone phosphate and NADPH 5% of that with NADH
-
additional information
Cagpd1p is a NAD+-dependent GPD, no activity with NADP+; Cagpd2p is a NAD+-dependent GPD, no activity with NADP+
-
additional information
Cagpd1p is a NAD+-dependent GPD, no activity with NADP+; Cagpd2p is a NAD+-dependent GPD, no activity with NADP+
-
additional information
A0A14OJW76
Cagpd1p is a NAD+-dependent GPD, no activity with NADP+; Cagpd2p is a NAD+-dependent GPD, no activity with NADP+
-
additional information
A0A14OJW77
Cagpd1p is a NAD+-dependent GPD, no activity with NADP+; Cagpd2p is a NAD+-dependent GPD, no activity with NADP+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
0.1-0.3 M, chloride salts become strongly inhibitory at higher concentrations, replacing K+ with Na+ or NH4+yields similar results
MgSO4
-
0.1-0.3 M, slight activation at low ionic strength, most inhibitory at higher concentration
NaCl
-
when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fructose-1,6-bisphosphate
-
at physiological concentration, non-competitive
glycerol phosphate
-
0.025 mM, strong inhibition of chloroplastic and cytosolic form, endproduct inhibition
gymnemic acid
-
may have some pharmacological activities including antidiabetic activity and lipid lowering effects via interaction with G3PDH
linoleic acid
-
0.003 mM, 40% inhibition of chloroplastic form and 43% inhibition of cytosolic form
octyl glucose
-
0.003 mM, 41% inhibition of chloroplastic form and 61% inhibition of cytosolic form
palmitic acid
-
0.003 mM, 40% inhibition of chloroplastic form and 43% inhibition of cytosolic form
phenylmethyl sulfonyl fluoride
-
0.5 mM 50% inhibition of cytosolic form, little effect on chloroplastic form
phosphatidyl choline
-
0.003 mM, 42% inhibition of chloroplastic form and 43% inhibition of cytosolic form
phosphite dianion
-
strongly inhibits the mutant N270A enzyme. The N270A mutation results in a change in the effect of phosphite dianion on (kcat/Km)obs for GPDH-catalyzed reduction of glycerone phosphate, from strongly activating to inhibiting
sedoheptulose 1,7-bisphosphate
-
0.5 mM, chloroplastic and cytosolic form inhibited by 50%
Triton X-100
-
0.006 mM, 50% inhibition of chloroplastic form and 52% inhibition of cytosolic form
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
-
trypanocidal drug, IC50 0.00055 mM
adenosine diphosphate ribose
-
0.094 mM slightly inhibits NADH binding by honeybee GPDH, but not by rabbit GPDH
Cl-
-
competitive inhibitor with respect to dihydroxyacetone phosphate
Cl-
-
cations, i.e. H+, K+, Na+ associated with Cl- do not affect the reduction of dihydroxyacetone phosphate
dihydroxyacetone phosphate
-
high levels of substrate, i.e. dihydroxyacetone phosphate result in inhibition
dihydroxyacetone phosphate
-
substrate inhibition above 1 mM, NADH above 0.2 mM; substrate inhibition only at high concentration, over 1 mM
L-glycerol 3-phosphate
-
competitive inhibitor to dihydroxyacetone phosphate, non-competitive to NADH
L-glycerol 3-phosphate
-
over 0.025 mM, strong inhibitor of cytosolic and chloroplastic enzyme
Melarsen oxide
-
active principle of the trypanocidal drug melarsoprol and cymelarsen
Melarsen oxide
-
active principle of the trypanocidal drug melarsoprol and cymelarsen; cymelarsen, IC50 0.0015-0.005 mM
N-ethylmaleimide
-
1 mM results in 50% inhibition, reversible by NADH, inhibition increases in the presence of dihydroxyacetone phosphate and/or glycerol 3-phosphate
N-ethylmaleimide
-
20 mM, complete inhibition; 20 mM, complete loss of activity
N-ethylmaleimide
-
reversible by dithiothreitol, 5 mM inhibits more than 90% of the enzyme activity
NaCl
isozyme GPDH1 is severely inhibited by the addition of 100-200 mM NaCl; isozyme GPDH2 is severely inhibited by the addition of 100-200 mM NaCl
NAD+
-
competitive inhibitor to NADH at physiological concentration; non-competitive to dihydroxyacetone phosphate
NAD+
-
competitive inhibitor to NADH at physiological concentration
NADPH
-
inhibits in presence of saturing concentration of NADH and dihydroxyacetone phosphate
NADPH
-
inhibits in presence of saturing concentration of NADH and dihydroxyacetone phosphate
p-chloromercuribenzoate
-
10 nM, strong inhibition; reversible by dithiothreitol, 0.001 mM inhibits more than 90% of the enzyme activity
phosphate
phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH1; phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH2
phosphate
-
competitive inhibitor against dihydroxyacetone phosphate, non-competitive inhibitor against NADH
phosphate
-
slight inhibition of cytosolic form, at higher concentrations above 20-30 mM both forms are inhibited
additional information
GPDH1 transcript level decreases progressively with NaCl concentrations above 3-5 M, the expression level of GPDH1 in 5 M NaCl is only approximately a quarter of that in 2 M NaCl; the GPDH2 transcript level decreases to less than half the level in 1 M NaCl
-
additional information
GPDH1 transcript level decreases progressively with NaCl concentrations above 3-5 M, the expression level of GPDH1 in 5 M NaCl is only approximately a quarter of that in 2 M NaCl; the GPDH2 transcript level decreases to less than half the level in 1 M NaCl
-
additional information
-
treatment with 0.075 mg/ml Ascophyllum nodosum extract depressed cellular GPDH activity by approximately 20%
-
additional information
-
coenzyme analogs: acetylpyridine-NAD+, deaminoacetylpyridine-NAD+, pyridinealdehyde-NAD+, deaminopyridinealdehyde-NAD+, potent inhibitors
-
additional information
no inhibition of the cytosolic NAD+-linked cGPDH enzyme by cell-permeant small-molecule inhibitors of mitochondrial mGPDH, EC 1.1.5.3, with a core benzimidazole-phenyl-succinamide structure
-
additional information
-
the hyperthyroid status leads to a significant decrease of both enzyme amount and activity in both female and male animals
-
additional information
-
no inhibition by NADPH, acetaldehyde, glycerol, ethanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dihydrolipoic acid
-
stimulation of chloroplastic form, 147% of enzyme activity
dithiothreitol
-
stimulation of chloroplastic form, 150% of enzyme activity
fructose 2,6-bisphosphate
-
0.025 mM maximum stimulation of 2.3fold of cytosolic form, not chloroplastic form, no stimulation by fructose-1,6-bisphosphate
glycerol
-
competitive activator with respect to dihydroxyacetone phosphate above 30 mM
potassium glutamate
-
up to 0.1 M, activation, high activity also at high ionic strength
phosphite dianion
-
strongly activates the wild-type enzyme. The N270A mutation results in a change in the effect of phosphite dianion on (kcat/Km)obs for GPDH-catalyzed reduction of glycerone phosphate, from strongly activating to inhibiting
phosphite dianion
-
allosteric activation. Separate binding of the second substrate piece phosphite dianion strongly activates GPDH for catalysis of the reduction of glycolaldehyde by NADH
additional information
the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of GPDH1 transcript reaches a maximum in 2 M NaCl, which is about 2fold more than that in 0.5 M NaCl; the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of isozyme GPDH2 transcript reaches a maximum in 1 M NaCl and although the GPDH2 transcript level almost remains constant in salinities ranging from 3 to 5 M NaCl
-
additional information
the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of GPDH1 transcript reaches a maximum in 2 M NaCl, which is about 2fold more than that in 0.5 M NaCl; the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of isozyme GPDH2 transcript reaches a maximum in 1 M NaCl and although the GPDH2 transcript level almost remains constant in salinities ranging from 3 to 5 M NaCl
-
additional information
-
the hypothyroid status to a significant increase of both enzyme amount and activity in both female and male animals
-
additional information
the enzyme shows higher enzymatic activity in response to osmotic and cold stress
-
additional information
-
the enzyme shows higher enzymatic activity in response to osmotic and cold stress
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2144
dihydroxyacetone phosphate
-
alpha-GPDHs, standard deviation 0.0215 mM
0.2
NAD+
-
enzyme from euthermic animal, at pH 7.5 and 22°C; enzyme from hibernating animal, at pH 7.5 and 22°C; pH 7.5, 22°C, euthermic G3PDH enzyme and hibernation G3PDH enzyme
0.32
NAD+
-
enzyme from hibernating animal, at pH 8.0 and 37°C; pH 8.0, 37°C, hibernation G3PDH enzyme
0.39
NAD+
-
enzyme from euthermic animal, at pH 8.0 and 37°C; pH 8.0, 37°C, euthermic G3PDH enzyme
0.42
NAD+
-
enzyme from hibernating animal, at pH 8.0 and 22°C; pH 8.0, 22°C, hibernation G3PDH enzyme
0.5
NAD+
-
enzyme from euthermic animal, at pH 7.5 and 37°C; pH 7.5, 37°C, euthermic G3PDH enzyme
0.52
NAD+
-
enzyme from euthermic animal, at pH 8.0 and 22°C; pH 8.0, 22°C, euthermic G3PDH enzyme
0.69
NAD+
-
enzyme from hibernating animal, at pH 7.5 and 37°C; pH 7.5, 37°C, hibernation G3PDH enzyme
0.001
NADH
-
pH 7.5, 22°C, liver isozyme; pH 7.5, 5°C, liver isozyme; pH 7.5, 5°C, muscle isozyme
0.41
sn-glycerol 3-phosphate
-
enzyme from hibernating animal, at pH 7.5 and 22°C; pH 7.5, 22°C, hibernation G3PDH enzyme
0.48
sn-glycerol 3-phosphate
-
enzyme from hibernating animal, at pH 8.0 and 5°C; pH 8.0, 5°C, hibernation G3PDH enzyme
0.57
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 8.0 and 22°C; pH 8.0, 22°C, euthermic G3PDH enzyme
0.61
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 7.5 and 22°C; pH 7.5, 22°C, euthermic G3PDH enzyme
0.63
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 7.5 and 37°C; pH 7.5, 37°C, euthermic G3PDH enzyme
0.83
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 8.0 and 5°C; pH 8.0, 5°C, euthermic G3PDH enzyme
0.88
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 8.0 and 37°C; pH 8.0, 37°C, euthermic G3PDH enzyme
1.17
sn-glycerol 3-phosphate
-
enzyme from hibernating animal, at pH 7.5 and 37°C; pH 7.5, 37°C, hibernation G3PDH enzyme
1.51
sn-glycerol 3-phosphate
-
enzyme from euthermic animal, at pH 7.5 and 5°C; pH 7.5, 5°C, euthermic G3PDH enzyme
1.56
sn-glycerol 3-phosphate
-
enzyme from hibernating animal, at pH 8.0 and 37°C; pH 8.0, 37°C, hibernation G3PDH enzyme
1.61
sn-glycerol 3-phosphate
-
enzyme from hibernating animal, at pH 8.0 and 22°C; pH 8.0, 22°C, hibernation G3PDH enzyme
additional information
alpha-glycerophosphate
-
Km values from five different isoelectric focused components
additional information
additional information
-
various Km-values of 4 isozymes of heart, muscle, liver and mammary gland
-
additional information
additional information
-
Km values of isozyme I5.9
-
additional information
additional information
-
Km values of two further allelic isozymes, alpha-GPDHf and alpha-GPDHm
-
additional information
additional information
-
Km values of isozyme GPDH-3
-
additional information
additional information
-
kinetic analysis, overview. Relative to euthermic liver G3PDH, hibernator liver G3PDH has a decreased affinity for its substrate, glycerol-3-phosphate, at 37°C and 22°C, while at 5°C, there is a significant increase in the affinity for G3P in the hibernating form of the enzyme, relative to the euthermic form. A change in pH from pH 8.0 to pH 7.5 leads to increased G3PDH affinity for NAD+. With a change in pH from pH 8.0 to pH 7.5 at 22°C in the euthermic and hibernator conditions, the Km for NAD+ decreases by 62% and 53%, respectively
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00028
dihydroxyacetone phosphate
-
mutant enzyme R269A/N270A, at pH 7.5 and 25°C
345
dihydroxyacetone phosphate
-
reduction of synthetic dihydroxyacetone phosphate, 20°C, pH 7, rabbit muscle
390
dihydroxyacetone phosphate
-
reduction of synthetic dihydroxyacetone phosphate, 20°C, pH 7, rabbit muscle, under conditions where competitive inhibition by fructose 1,6-diphosphate are not excluded
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000003
glycolaldehyde
-
mutant enzyme R269A, at pH 7.5 and 25°C; mutant enzyme R269A/N270A, at pH 7.5 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(-)-epigallocatechin-3-gallate
-
substrate dihydroxyacetone phosphate, pH 7.4, 25°C; substrate NADH, pH 7.4, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00055
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
Leishmania mexicana
-
trypanocidal drug, IC50 0.00055 mM
0.57
guanidine hydrochloride
Urocitellus richardsonii
-
enzyme from hibernating animal, at pH 7.5 and 22°C
0.69
guanidine hydrochloride
Urocitellus richardsonii
-
enzyme from euthermic animal, at pH 7.5 and 22°C
0.57
guanidinium hydrochloride
Urocitellus richardsonii
-
pH 8.0, 22°C, hibernation G3PDH enzyme
0.69
guanidinium hydrochloride
Urocitellus richardsonii
-
pH 8.0, 22°C, euthermic G3PDH enzyme
1.8
Urea
Urocitellus richardsonii
-
enzyme from hibernating animal, at pH 7.5 and 22°C; pH 8.0, 22°C, hibernation G3PDH enzyme
2.22
Urea
Urocitellus richardsonii
-
enzyme from euthermic animal, at pH 7.5 and 22°C; pH 8.0, 22°C, euthermic G3PDH enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
77
-
isozyme I6.5, after affinity chromatography, after preparative isoelectric-focusing: 175 units/mg
119
-
62 units/mg calculated by using protein concentration determined by dry-weight measurements
234
-
adipose tissue,147 units/mg refer to protein determination by Kjeldahl nitrogen analysis
additional information
-
activities with the different isozymes at different temperatures, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.6
6.8
7.2
-
reduction of dihydroxyacetone phosphate, purified enzyme, decline in activity is more rapid at higher pH values, 7.3-7.5 crude homogenate of enzyme
7.5
8.5
9.3
9.6
additional information
-
optimum pH values for components P-I, P-II, PIV, P-V range between pH 8.2 and 8.6, liver
7.5
-
reduction of dihydroxyacetone phosphate, in 0.2 M phosphate buffer
9.3
-
liver, component P-III, pH optimum of testis enzyme also around pH 9.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.1
-
about half-maximal activity at pH 5.0 and 8.1, reduction of dihydroxyacetone phosphate
5.2 - 7.8
-
about half-maximal activity between pH 5.2 and 7.8, reduction of dihydroxyacetone phosphate
5.8 - 7.2
-
reduction of dihydroxyacetone phosphate occurs over a broad range between 5.8 to 7.2
6 - 6.5
-
maximal activities of the three allelic forms are obtained within a pH range of 6.0-6.5 for dihydroxyacetone phosphate reduction
6.5 - 8.2
-
about half-maximal activity at pH 6.5 and 8.2, reduction of dihydroxyacetone phosphate
6.7 - 8.7
-
about 80% of maximal activity at pH 6.7 and 8.7, reduction of dihydroxyacetone phosphate, decrease of activity below and above these pH values
7 - 8
-
dihydroxyacetone reduction, activity decreases rapidly below pH 7.0 and above pH 8.0, more rapidly at acidic values
7.5 - 8
-
pH-rate profile for the reduction of dihydroxyacetone phosphate shows rather sharp optimum between pH 7.5 and 8.0
8 - 11
-
about half-maximal activity at pH 8.0 and 11.0, oxidation of L-glycerol-3-phosphate
8 - 10
-
about half-maximal activity at pH 8.0 and 10.0, oxidation of glycerol 3-phosphate, isozymes P-III, liver
8.1 - 9.4
-
about 80% of maximal activity at pH 8.1 and 9.4, oxidation of glycerol-3-phosphate, decrease of activity below and rapidly above these pH values
8.6 - 10
-
about half-maximal activity at pH 8.6 and 10.0, oxidation of glycerol 3-phosphate
10 - 10.5
-
maximal activities of the three allelic forms are obtained within a pH range of 10.0-10.5 for glycerol 3-phosphate oxidation
additional information
-
A change in pH from pH 8.0 to pH 7.5 leads to increased G3PDH affinity for NAD+. With a change in pH from pH 8.0 to pH 7.5 at 22°C in the euthermic and hibernator conditions, the Km for NAD+ decreases by 62% and 53%, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
; and longissimus dorsi muscle, similar expression pattern that is at a low level at birth and increasing with aging to the highest level at postnatal day 8 in longissinus doris muscle and postnatal day 14 in cerebrum. Weaning decreases the expression level of the GPD1 gene
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A