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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
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

-
Drosophila GPDH-1-null mutants cannot fly
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
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
-
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
D2XN65
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
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 enzyme is important for osmotolerance
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
-
the enzyme is important for osmotolerance
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
dihydroxyacetone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
?
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 1-phosphate + NAD+
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
glycerone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
r
glycerone phosphate + NADH
L-glycerol-3-phosphate + NAD+
-
-
-
-
r
glycerone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
-
-
-
-
r
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
glycolaldehyde + NADH + H+
?
-
-
-
-
?
glycolaldehyde + NADH + H+
? + NAD+
-
truncated substrate
-
-
r
glycolaldehyde + NADH + H+
ethane-1,2-diol + NAD+
-
-
-
-
r
L-glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
additional information
?
-
dihydroxyacetone phosphate + NADH

glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
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+
-
-
-
-
?
glycerol-3-phosphate + NAD+

glycerone phosphate + NADH
-
-
-
-
r
glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
-
-
-
-
?
glycerone phosphate + NADH + H+

sn-glycerol 3-phosphate + NAD+
-
-
-
r
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+
-
-
-
-
?
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
r
glycolaldehyde + NADH

?
-
-
-
-
?
glycolaldehyde + NADH
?
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
-
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+
-
-
-
-
?
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 + 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+
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
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+
D2XN65
-
-
-
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
?
-
no activity with NADP+
-
-
-
additional information
?
-
no activity with NADP+
-
-
-
additional information
?
-
A0A14OJW76
no activity with NADP+
-
-
-
additional information
?
-
A0A14OJW77
no activity with NADP+
-
-
-
additional information
?
-
no activity with NADP+
-
-
-
additional information
?
-
no activity with NADP+
-
-
-
additional information
?
-
A0A14OJW76
no activity with NADP+
-
-
-
additional information
?
-
A0A14OJW77
no activity with NADP+
-
-
-
additional information
?
-
-
no activity with NADP+
-
-
-
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
?
-
-
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
?
-
-
glyceraldehyde-3-phosphate
-
-
-
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
?
-
-
-
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
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
?
-
-
glycerol
-
-
-
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 GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
-
additional information
?
-
-
glycerol
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
glycerol
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
DL-glyceraldehyde, phosphohydroxypyruvate
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
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.
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 1-phosphate + NAD+
Q949Q0
-
-
-
r
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
additional information
?
-
dihydroxyacetone phosphate + NADH

glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
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
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
-
?
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+
-
-
-
-
?
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+
Q52ZA0, V9MH41
-
-
-
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+
-
-
-
-
?
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+
D2XN65
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-epigallocatechin-3-gallate
-
noncompetitive
2,3-Dimercaptopropanol
-
competitive inhibitor to glycerophosphate
2,4-Dichlorophenoxyacetic acid
-
-
2-amino-2-hydroxymethylpropane-1,3-diol
-
i.e. Tris
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
3-morpholinosydnonimine
-
-
adenosine diphosphate ribose
ADP
-
at physiological concentration, 10 mM 90% inhibition
ADP-ribose
-
allosteric inhibitor
Cd2+
-
50% inhibition at 8.33 mM; 50% inhibition at 8.3 mM
Cu2+
-
50% inhibition at 12.96 mM; 50% inhibition at 13.0 mM
dihydroxyacetone phosphate
FeCl2
-
0.5 mM, about 10% residual activity
fructose-1,6-bisphosphate
-
at physiological concentration, non-competitive
glycerol
-
slight inhibition
glycerol phosphate
-
0.025 mM, strong inhibition of chloroplastic and cytosolic form, endproduct inhibition
guanidine hydrochloride
-
-
guanidinium hydrochloride
-
-
gymnemic acid
-
may have some pharmacological activities including antidiabetic activity and lipid lowering effects via interaction with G3PDH
iodoacetamide
-
effective inhibitor
K+
-
50% inhibition at 40.66 mM; 50% inhibition at 40.7 mM
Large peptide factor
-
chloroplast enzyme
-
linoleic acid
-
0.003 mM, 40% inhibition of chloroplastic form and 43% inhibition of cytosolic form
malate
-
at high concentration
Mn2+
-
50% inhibition at 36.6 mM
NADH-X
-
allosteric inhibitor
Ni2+
-
50% inhibition at 31.66 mM; 50% inhibition at 31.7 mM
Nucleic acids
-
strongly inhibit
-
o-Iodosobenzoic acid
-
0.5 mM, about 10% residual activity
octyl glucose
-
0.003 mM, 41% inhibition of chloroplastic form and 61% inhibition of cytosolic form
p-mercuribenzoate
-
0.1 mM complete inhibition
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
phosphogluconate
-
cytosolic isozyme
reduced thioredoxin
-
stimulation of chloroplastic form
S-nitroso-N-acetylpenicillamine
-
-
sedoheptulose 1,7-bisphosphate
-
0.5 mM, chloroplastic and cytosolic form inhibited by 50%
selenocysteine
-
0.015 mM, 10% residual activity
selenomethionine
-
0.015 mM, 40% residual activity
Small peptide factor
-
cytosolic enzyme
-
SO42-
-
at high concentration, MgSO4 most inhibitory
Sodium selenite
-
0.015 mM, 10% residual activity
Thylakoid fraction
-
0.02 mM 97% inhibition
-
Triton X-100
-
0.006 mM, 50% inhibition of chloroplastic form and 52% inhibition of cytosolic form
Zn2+
-
50% inhibition at 5.66 mM; 50% inhibition at 5.7 mM
ZnCl2
-
0.5 mM, about 10% residual activity
(NH4)2SO4

-
-
(NH4)2SO4
-
inhibition of chloroplastic and cytosolic form
2-hydroxy-1,2,3-nonadecanetricarboxylic acid

-
trypanocidal drug, IC50 0.00055 mM
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
-
IC50 0.0011 mM
adenosine diphosphate ribose

-
0.094 mM slightly inhibits NADH binding by honeybee GPDH, but not by rabbit GPDH
adenosine diphosphate ribose
-
-
ATP

-
weak inhibitor of both isozymes, i.e. GPDH-1 and -3
ATP
-
at physiological concentration, 10 mM 95% inhibition
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
dihydroxyacetone phosphate
-
0.5 mM, GPDHs more susceptible to inhibition
dihydroxyacetone phosphate
-
substrate inhibition at 0.2 mM
dihydroxyacetone phosphate
-
substrate inhibition at 0.2 mM
iodoacetate

-
-
iodoacetate
-
50 mM, incubated for 60 min
iodoacetate
-
0.1 mM 23% inhibition
iodoacetate
-
reversible by dithiothreitol, 10 mM inhibits to 50%
L-glycerol 3-phosphate

-
inhibits dihydroxyacetone phosphate reduction
L-glycerol 3-phosphate
-
-
L-glycerol 3-phosphate
-
inhibitor of bumble bee enzyme, non-competitive
L-glycerol 3-phosphate
-
competitive inhibitor to dihydroxyacetone phosphate, non-competitive to NADH
L-glycerol 3-phosphate
-
inhibits dihydroxyacetone phosphate reduction
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

-
0.1 mM inhibits enzyme over 60%
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
-
0.5 mM, about 20% residual activity
N-ethylmaleimide
-
20 mM, complete inhibition; 20 mM, complete loss of activity
N-ethylmaleimide
-
0.1 mM complete inhibition
N-ethylmaleimide
-
reversible by dithiothreitol, 5 mM inhibits more than 90% of the enzyme activity
NaCl

-
inactivation
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
NaCl
-
strongly inhibits, 50% activity at 250 mM NaCl
NaCl
-
inactivates irreversibly
NaCl
-
strongly inhibits, 50% activity at 250 mM NaCl
NAD+

-
competitive inhibitor to NADH at physiological concentration; non-competitive to dihydroxyacetone phosphate
NAD+
-
competitive inhibitor to NADH at physiological concentration
NAD+
-
competitive inhibitor to NADH at physiological concentration
NADH

-
at high concentration
NADH
-
at high concentration
NADPH

-
-
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

-
0.0001 mM inhibits enzyme over 60%
p-chloromercuribenzoate
-
0.05 mM, 100% inhibition
p-chloromercuribenzoate
-
effective inhibitor
p-chloromercuribenzoate
-
10 nM, strong inhibition
p-chloromercuribenzoate
-
10 nM, strong inhibition; reversible by dithiothreitol, 0.001 mM inhibits more than 90% of the enzyme activity
p-chloromercuribenzoate
-
0.1 mM, reversed by thiols, e.g. dithiothreitol
phosphate

-
competitive inhibition
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
suramin

-
trypanocidal drug, potent inhibitor, IC50 0.0002 mM
suramin
-
IC50 0.00044 mM
additional information

-
high ionic strength above 0.03 M
-
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
-
not inhibitory: CaCl2, MgCl2, 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
-
additional information
-
-
-
additional information
-
cyclic-AMP
-
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0.3
alpha-glycerol phosphate
-
-
0.11 - 3.39
alpha-glycerophosphate
0.012 - 25
dihydroxyacetone phosphate
0.19 - 1.2
DL-glycerol-3-phosphate
0.59 - 2
glycerol 3-phosphate
1.6
glycerol phosphate
-
-
0.468 - 34
glycerol-3-phosphate
0.137
Glycerone
-
pH 7.6, 25°C
0.052 - 137
glycerone phosphate
0.74
L-glycerol 3-phosphate
-
-
2.3 - 3.9
L-glycerol-3-phosphate
0.41 - 469
sn-glycerol 3-phosphate
0.143
sn-glycerol-3-phosphate
-
measured at pH 9.0
additional information
alpha-glycerophosphate
0.11
alpha-glycerophosphate

-
-
0.33
alpha-glycerophosphate
-
testes
3.39
alpha-glycerophosphate
-
liver
0.012
dihydroxyacetone phosphate

-
-
0.026
dihydroxyacetone phosphate
-
measured at pH 7.5
0.052
dihydroxyacetone phosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.075
dihydroxyacetone phosphate
-
-
0.1
dihydroxyacetone phosphate
-
-
0.12
dihydroxyacetone phosphate
-
-
0.13
dihydroxyacetone phosphate
-
standard deviation 0.03 mM
0.15
dihydroxyacetone phosphate
-
muscle
0.17
dihydroxyacetone phosphate
-
-
0.2
dihydroxyacetone phosphate
-
I6.5
0.2144
dihydroxyacetone phosphate
-
alpha-GPDHs, standard deviation 0.0215 mM
0.23
dihydroxyacetone phosphate
-
in MOPS buffer, 0.33 mM in Tris-histidine
0.23
dihydroxyacetone phosphate
-
-
0.25
dihydroxyacetone phosphate
-
adipose tissue
0.3
dihydroxyacetone phosphate
-
0.30-0.35 mM
0.33
dihydroxyacetone phosphate
-
-
0.46
dihydroxyacetone phosphate
-
-
0.52
dihydroxyacetone phosphate
-
GPDH-1
0.54
dihydroxyacetone phosphate
-
-
0.54
dihydroxyacetone phosphate
at pH 7.0 and 25°C
0.61
dihydroxyacetone phosphate
at pH 7.0 and 25°C
5.7
dihydroxyacetone phosphate
-
mutant enzyme R269A, at pH 7.5 and 25°C
15
dihydroxyacetone phosphate
-
mutant enzyme R269A/N270A, at pH 7.5 and 25°C
25
dihydroxyacetone phosphate
-
mutant enzyme N270A, at pH 7.5 and 25°C
0.19
DL-glycerol-3-phosphate

-
muscle
0.3
DL-glycerol-3-phosphate
-
I6.5
0.4
DL-glycerol-3-phosphate
-
adipose tissue
1.2
DL-glycerol-3-phosphate
-
standard deviation 0.5 mM
0.59
glycerol 3-phosphate

-
GPDH-1
0.909
glycerol 3-phosphate
-
-
1.89
glycerol 3-phosphate
-
alpha-GPDHs, standard deviation 0.25 mM
2
glycerol 3-phosphate
-
-
0.468
glycerol-3-phosphate

-
pH 9.0, 25°C
1.7
glycerol-3-phosphate
-
-
2.25
glycerol-3-phosphate
-
-
34
glycerol-3-phosphate
-
isoform Gut2, pH 6.8
0.052
glycerone phosphate

-
wild-type enzyme, pH 7.5, 25°C
0.154
glycerone phosphate
-
pH 7.5, 5°C, muscle isozyme
0.259
glycerone phosphate
-
pH 7.5, 5°C, liver isozyme
0.26
glycerone phosphate
-
pH 7.5, 25°C
0.279
glycerone phosphate
-
pH 7.5, 22°C, muscle isozyme
0.352
glycerone phosphate
-
pH 7.5, 22°C, liver isozyme
1.5
glycerone phosphate
-
mutant R269A/N270A, pH 7.5, 25°C
2.5
glycerone phosphate
-
mutant N270A, pH 7.5, 25°C
5.7
glycerone phosphate
-
mutant R269A, pH 7.5, 25°C
137
glycerone phosphate
-
pH 9.0, 25°C
2.3
L-glycerol-3-phosphate

-
pH 10.0, 25°C
3.9
L-glycerol-3-phosphate
-
pH 7.5, 25°C
0.0044
NAD+

-
adipose tissue
0.036
NAD+
-
measured at pH 9.0
0.045
NAD+
-
pH 8.5, 22°C, liver isozyme
0.09
NAD+
-
pH 8.5, 5°C, liver isozyme
0.09
NAD+
-
pH 8.0, 5°C, hibernation G3PDH enzyme
0.1003
NAD+
-
alpha-GPDHs, standard deviation 0.0041 mM
0.12
NAD+
-
pH 8.0, 5°C, euthermic G3PDH enzyme
0.143
NAD+
-
pH 8.5, 22°C, muscle isozyme
0.155
NAD+
-
pH 8.5, 5°C, muscle isozyme
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
0.3
NAD+
-
standard deviation 0.06 mM
0.316
NAD+
-
pH 9.0, 25°C
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
0.003
NADH
-
pH 7.5, 22°C, muscle isozyme
0.0043
NADH
-
adipose tissue
0.005
NADH
-
measured at pH 7.5
0.005
NADH
-
pH 7.5, 25°C
0.00526
NADH
-
alpha-GPDHs
0.0066
NADH
-
standard deviation 0.003 mM
0.01
NADH
-
less than 0.01 mM
0.01
NADH
-
less than 0.01 mM
0.032
NADH
-
pH 7.6, 25°C
0.051
NADH
at pH 7.0 and 25°C
0.0589
NADH
recombinant isozyme GDH2
0.0592
NADH
isozyme GPDH2
0.0905
NADH
isozyme GPDH1; recombinant isozyme GDH1
0.11
NADH
at pH 7.0 and 25°C
0.0589
NADPH

isozyme GPDH1
0.0592
NADPH
recombinant isozyme GDH1
0.0726
NADPH
isozyme GPDH2; recombinant isozyme GDH2
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
469
sn-glycerol 3-phosphate
-
pH 7.6, 25°C
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
-
Michaelis-Menten kinetics
-
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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