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Information on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+)
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EC Tree
1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)IUBMB Comments
Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
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Word Map
- 1.1.1.8
- adipose
- adipocytes
- glyceraldehyde-3-phosphate
-
preadipocytes
- glyceraldehyde
-
lipogenic
-
adipogenesis
- dhap
-
omental
-
alpha-gpdh
-
perirenal
-
allozyme
-
fad-linked
- synthesis
- nutrition
- biotechnology
- medicine
- food industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
(NAD+)-dependent G3pdh, (NAD+)-dependent glycerol-3-phosphate dehydrogenase, alpha glycerophosphate dehydrogenase, alpha-glycerol phosphate dehydrogenase (NAD), alpha-glycerophosphate dehydrogenase (NAD), Cagpd1, Cagpd1p, Cagpd2, Cagpd2p, cG3PDH, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(NAD+)-dependent G3pdh
(NAD+)-dependent glycerol-3-phosphate dehydrogenase
alpha-glycerol phosphate dehydrogenase (NAD)
-
-
-
-
alpha-glycerophosphate dehydrogenase (NAD)
-
-
-
-
Cagpd1
Cagpd2
cGPdH
cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase
dehydrogenase, glycerol phosphate
-
-
-
-
DhGPD1
G3PD1
G3PD2
G3PD3
G3PDH
glycerol 1-phosphate dehydrogenase
-
-
-
-
glycerol 3-phosphate dehydrogenase
glycerol phosphate dehydrogenase (NAD)
-
-
-
-
glycerol-3-phosphate dehydrogenase
glycerol-3-phosphate dehydrogenase 1
glycerophosphate dehydrogenase (NAD)
-
-
-
-
GPD
GPD1
Gpd1p
gpd2p
GPDH
GPDH-1
GPDH-2
GPDH1
GPDH2
hydroglycerophosphate dehydrogenase
-
-
-
-
L-alpha-glycerol phosphate dehydrogenase
-
-
-
-
L-alpha-glycerophosphate dehydrogenase
-
-
-
-
L-glycerol phosphate dehydrogenase
-
-
-
-
L-glycerophosphate dehydrogenase
-
-
-
-
mGPDH
NAD+-dependent G3P dehydrogenase
NAD+-dependent glycerol-3-phosphate dehydrogenase
NAD+-GPDH
NAD-alpha-glycerophosphate dehydrogenase
-
-
-
-
NAD-dependent glycerol phosphate dehydrogenase
-
-
-
-
NAD-dependent glycerol-3-phosphate dehydrogenase
NAD-L-glycerol-3-phosphate dehydrogenase
-
-
-
-
NAD-linked glycerol 3-phosphate dehydrogenase
-
-
-
-
NADH-dihydroxyacetone phosphate reductase
-
-
-
-
NADP+-dependent glycerol 3-phosphate dehydrogenase
-
GPDH-2
isozyme GPDH-2 provides precursors for lipid biosynthesis in many tissues
GPDH1
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
GPDH1
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
-
GPDH2
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
GPDH2
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
-
NAD-dependent glycerol-3-phosphate dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
-
-
-
-
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
ordered bi-bi mechanism
-
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+
-
-
-
-
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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+
-
-
-
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+
dihydroxyacetone 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+
-
-
-
-
?
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 + 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 + 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
-
-
-
additional information
?
-
no activity with NADP+
-
-
-
additional information
?
-
no activity with NADP+
-
-
-
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NATURAL SUBSTRATE
NATURAL 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 + 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
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+
-
-
-
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+
-
-
-
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+
-
-
-
-
?
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+
-
-
-
?
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
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
?
-
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+
-
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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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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenoma, Bile Duct
Enzyme histochemical and immunohistochemical characterization of oval and parenchymal cells proliferating in livers of rats fed a choline-deficient/DL-ethionine-supplemented diet.
Adenoma, Liver Cell
Enzyme histochemical and immunohistochemical characterization of oval and parenchymal cells proliferating in livers of rats fed a choline-deficient/DL-ethionine-supplemented diet.
Anemia, Sickle Cell
Decreased G3PDH binding to erythrocyte membranes in sickle cell disease.
Arthritis
Oxidation of articular cartilage glyceraldehyde-3-phosphate dehydrogenase (G3PDH) occurs in vivo during carrageenin-induced arthritis.
Atherosclerosis
[Structure of cytoplasmic glycerol-3-phosphate dehydrogenase in experimental atherosclerosis in rabbits]
beta-Thalassemia
Glycerol-3-phosphate dehydrogenase activity in the red cells of patients with thalassemia.
Breast Neoplasms
Comparative Proteome Analysis of Breast Cancer Tissues Highlights the Importance of Glycerol-3-phosphate Dehydrogenase 1 and Monoacylglycerol Lipase in Breast Cancer Metabolism.
Breast Neoplasms
Identification of glycerol-3-phosphate dehydrogenase 1 as a tumour suppressor in human breast cancer.
Carcinoma, Ehrlich Tumor
Changes in enzyme pattern of Ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content.
Carcinoma, Hepatocellular
Proportional activities of glycerol kinase and glycerol 3-phosphate dehydrogenase in rat hepatomas.
Chagas Disease
Differential tissue and flight developmental expression of glycerol-3-phosphate dehydrogenase isozymes in the Chagas disease vector Triatoma infestans.
Cholestasis, Intrahepatic
Effects of supplementation on food intake, body weight and hepatic metabolites in the citrin/mitochondrial glycerol-3-phosphate dehydrogenase double-knockout mouse model of human citrin deficiency.
Citrullinemia
Effects of supplementation on food intake, body weight and hepatic metabolites in the citrin/mitochondrial glycerol-3-phosphate dehydrogenase double-knockout mouse model of human citrin deficiency.
Dehydration
Cell wall involvement in the glycerol response to high osmolarity in the halotolerant yeast Debaryomyces hansenii.
Dehydration
Dehydration of a phosphonate substrate analogue by glycerol 3-phosphate dehydrogenase.
Diabetes Mellitus
Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus.
Diabetes Mellitus
Molecular cloning of human mitochondrial glycerophosphate dehydrogenase gene: genomic structure, chromosomal localization, and existence of a pseudogene.
Diabetes Mellitus, Experimental
Adaptive changes of glycerol 3-phosphate dehydrogenase level in rat skin: effects of starvation, alloxan diabetes and insulin.
Diabetes Mellitus, Type 2
Detection of variants in the mitochondrial glycerophosphate dehydrogenase gene in Japanese NIDDM patients.
Diabetes Mellitus, Type 2
Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells.
Diabetes Mellitus, Type 2
Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus.
Diabetes Mellitus, Type 2
Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker.
Dyslipidemias
Low abdominal subcutaneous preadipocyte adipogenesis is associated with visceral obesity, visceral adipocyte hypertrophy, and a dysmetabolic state.
Fatty Liver
Some lipogenic enzyme activities in rat livers in which an excessive fat accumulation occurred due to feeding low-level amino acid mixture diets.
Fatty Liver
The role of glycerol-3-phosphate dehydrogenase 1 in the progression of fatty liver after acute ethanol administration in mice.
Fatty Liver
Transient infantile hypertriglyceridemia, fatty liver, and hepatic fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate dehydrogenase 1.
glycerol-3-phosphate dehydrogenase (nad+) deficiency
Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells.
glycerol-3-phosphate dehydrogenase (nad+) deficiency
Expanding the molecular diversity and phenotypic spectrum of glycerol 3-phosphate dehydrogenase 1 deficiency.
glycerol-3-phosphate dehydrogenase (nad+) deficiency
Glycerol 3-phosphate dehydrogenase 1 deficiency enhances exercise capacity due to increased lipid oxidation during strenuous exercise.
glycerol-3-phosphate dehydrogenase (nad+) deficiency
Glycerol-3-phosphate dehydrogenase 1 deficiency induces compensatory amino acid metabolism during fasting in mice.
Head and Neck Neoplasms
[The cytochemical determination of alpha-glycerophosphate dehydrogenase and adenosine triphosphatase in the peripheral blood lymphocytes of patients with hepatobiliary system pathology]
Hepatitis
[The cytochemical determination of alpha-glycerophosphate dehydrogenase and adenosine triphosphatase in the peripheral blood lymphocytes of patients with hepatobiliary system pathology]
Hyperthyroidism
Thyroxine and tri-iodothyronine differently affect uncoupling protein-1 content and antioxidant enzyme activities in rat interscapular brown adipose tissue.
Hypertriglyceridemia
A novel homozygous mutation in the glycerol-3-phosphate dehydrogenase 1 gene in a Chinese patient with transient infantile hypertriglyceridemia: a case report.
Hypertriglyceridemia
Transient infantile hypertriglyceridemia, fatty liver, and hepatic fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate dehydrogenase 1.
Hypoglycemia
Naloxone, but not valsartan, preserves responses to hypoglycemia after antecedent hypoglycemia: Role of metabolic reprogramming in counterregulatory failure.
Infections
Effect of mitochondrial and/or cytosolic glycerol 3-phosphate dehydrogenase overexpression on glucose-stimulated insulin secretion from MIN6 and HIT cells.
Infections
Establishment of a quiescent herpes simplex virus type 1 infection in neurally-differentiated PC12 cells.
Insulin Resistance
Glycerol-3-phosphate dehydrogenase activity in human lymphocytes: effects of insulin, obesity and weight loss.
Insulinoma
Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker.
Intellectual Disability
Haploinsufficiency of the GPD2 gene in a patient with nonsyndromic mental retardation.
Leiomyoma
Expression of exon 5 deleted estrogen receptor variant messenger RNA in human uterine myometrium and leiomyoma.
Leukemia
KIS induces proliferation and the cell cycle progression through the phosphorylation of p27Kip1 in leukemia cells.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Detection of messenger RNA in leukocytes or plasma of patients with chronic myeloid leukemia.
Leukemia, Myeloid
KIS induces proliferation and the cell cycle progression through the phosphorylation of p27Kip1 in leukemia cells.
Liver Diseases
Deficiency of the mitochondrial glycerol 3-phosphate dehydrogenase contributes to hepatic steatosis.
Liver Neoplasms, Experimental
Proportional activities of glycerol kinase and glycerol 3-phosphate dehydrogenase in rat hepatomas.
Lung Diseases, Interstitial
Chemokine gene expression and clonal analysis of B cells in tissues involved by lymphoid interstitial pneumonitis from HIV-infected pediatric patients.
Metabolism, Inborn Errors
Expanding the molecular diversity and phenotypic spectrum of glycerol 3-phosphate dehydrogenase 1 deficiency.
Microphthalmos
Brachyury-related transcription factor Tbx2 and repression of the melanocyte-specific TRP-1 promoter.
Myelodysplastic Syndromes
KIS induces proliferation and the cell cycle progression through the phosphorylation of p27Kip1 in leukemia cells.
Neoplasms
Changes in enzyme pattern of Ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content.
Neoplasms
Expression of exon 5 deleted estrogen receptor variant messenger RNA in human uterine myometrium and leiomyoma.
Neoplasms
Glyceraldehyde-3-phosphate dehydrogenase mRNA expression in hepatocellular carcinoma.
Neoplasms
GPD1 enhances the anti-cancer effects of metformin by synergistically increasing total cellular glycerol-3-phosphate.
Neoplasms
Identification of glycerol-3-phosphate dehydrogenase 1 as a tumour suppressor in human breast cancer.
Neoplasms
Increased expression of mitochondrial glycerophosphate dehydrogenase and antioxidant enzymes in prostate cancer cell lines/cancer.
Neoplasms
Metformin Targets Mitochondrial Glycerophosphate Dehydrogenase to Control Rate of Oxidative Phosphorylation and Growth of Thyroid Cancer In Vitro and In Vivo.
Neoplasms
The reversible expression of an adult isozyme locus, Gdc-1, in tumors of the mouse.
Non-alcoholic Fatty Liver Disease
Deficiency of the mitochondrial glycerol 3-phosphate dehydrogenase contributes to hepatic steatosis.
Obesity
Association Between Cytosolic Glycerol 3-Phosphate Dehydrogenase Gene Expression in Human Subcutaneous Adipose Tissue and BMI.
Obesity
Enhanced glycerol 3-phosphate dehydrogenase activity in adipose tissue of obese humans.
Obesity
Mitochondrial glycerol 3-phosphate dehydrogenase promotes skeletal muscle regeneration.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
KIS induces proliferation and the cell cycle progression through the phosphorylation of p27Kip1 in leukemia cells.
Prostatic Neoplasms
High activity of mitochondrial glycerophosphate dehydrogenase and glycerophosphate-dependent ROS production in prostate cancer cell lines.
Prostatic Neoplasms
Increased expression of mitochondrial glycerophosphate dehydrogenase and antioxidant enzymes in prostate cancer cell lines/cancer.
Prostatic Neoplasms
Simultaneous detection of circulating prostate specific antigen (PSA)-expressing and prostate specific membrane antigen (PSM)-expressing cells by a multiplex reverse transcriptase polymerase chain reaction (RT-PCR) assay.
Seizures
Induction of glycerol phosphate dehydrogenase gene expression during seizure and analgesia.
Sleep Apnea, Obstructive
The influence of obstructive sleep apnea on the expression of glycerol-3-phosphate dehydrogenase 1 gene.
Starvation
Adaptive changes of glycerol 3-phosphate dehydrogenase level in rat skin: effects of starvation, alloxan diabetes and insulin.
Starvation
Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver.
Starvation
The effect of iron limitation on glycerol production and expression of the isogenes for NAD(+)-dependent glycerol 3-phosphate dehydrogenase in Saccharomyces cerevisiae.
Thymoma
Expression of cardiac insulin signalling genes and proteins in rats fed a high-sucrose diet: effect of bilberry anthocyanin extract.
Thyroid Neoplasms
Metformin Targets Mitochondrial Glycerophosphate Dehydrogenase to Control Rate of Oxidative Phosphorylation and Growth of Thyroid Cancer In Vitro and In Vivo.
Urinary Bladder Neoplasms
Increased activity of glycerol 3-phosphate dehydrogenase and other lipogenic enzymes in human bladder cancer.
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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
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
77
-
isozyme I6.5, after affinity chromatography, after preparative isoelectric-focusing: 175 units/mg
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
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
5 - 7.5
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 - 10
-
about half-maximal activity at pH 8.0 and 10.0, oxidation of glycerol 3-phosphate, isozymes P-III, liver
8 - 11
-
about half-maximal activity at pH 8.0 and 11.0, oxidation of L-glycerol-3-phosphate
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
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; an osmotolerant yeast isolated from soil outside a food factory
UniProt
brenda
; an osmotolerant yeast isolated from soil outside a food factory
UniProt
brenda
-
-
-
brenda
inbred Lewis strain euthyroid, hyperthyroid and hypothyroid male and female rats
-
-
brenda
-
-
-
brenda
overexprssion of glycerol-3-phosphate dehydrogenase results in the production of more glycerol and less ethanol during fermentation
-
-
brenda
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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
brenda
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
brenda