Information on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+)

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

EC NUMBER
COMMENTARY
1.1.1.8
-
RECOMMENDED NAME
GeneOntology No.
glycerol-3-phosphate dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
show the reaction diagram
ordered bi-bi mechanism
-
sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
one active site per enzyme molecule
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
equilibrium random-bi-bi reaction mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
ordered ternary-complex mechanism, NADH binds first
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
equilibrium random-bi-bi reaction mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
ordered bi-bi mechanism
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
equilibrium random-bi-bi reaction mechanism
Chlamydomonas reinhardtii 11/32-90, Saccharomyces cerevisiae YSH 11-6B
-
-
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
glycerol-3-phosphate shuttle
-
Glycerophospholipid metabolism
-
superpathway phosphatidate biosynthesis (yeast)
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(NAD+)-dependent G3pdh
-
-
(NAD+)-dependent G3pdh
Dunaliella salina 435
-
-
-
(NAD+)-dependent glycerol-3-phosphate dehydrogenase
-
-
(NAD+)-dependent glycerol-3-phosphate dehydrogenase
Dunaliella salina 435
-
-
-
alpha glycerophosphate dehydrogenase
-
-
alpha-glycerol phosphate dehydrogenase (NAD)
-
-
-
-
alpha-glycerophosphate dehydrogenase (NAD)
-
-
-
-
cG3PDH
-
-
cGPdH
Rattus norvegicus Lou/C
-
-
-
cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase
-
-
cytoplasmic NAD-dependent glycerol-3-phosphate dehydrogenase
Rattus norvegicus Lou/C
-
-
-
dehydrogenase, glycerol phosphate
-
-
-
-
DhGPD1
Q6VPR1
-
G-3-P dehydrogenase
O22216
-
G3P dehydrogenase
-
-
G3PDH
Dunaliella salina 435
-
-
-
glycerol 1-phosphate dehydrogenase
-
-
-
-
glycerol 3-phosphate dehydrogenase 1
-
-
glycerol phosphate dehydrogenase (NAD)
-
-
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
Chlamydomonas reinhardtii CC-125
-
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
Dunaliella salina 435
-
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase
Q00055
-
glycerol-3-phosphate dehydrogenase
-
-
glycerol-3-phosphate dehydrogenase 1
-
-
glycerol-3-phosphate dehydrogenase 1
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
glycerophosphate dehydrogenase (NAD)
-
-
-
-
GPD1
-
-
GPD1
-, D2XN65
-
GPD1
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
GPDH
Chlamydomonas reinhardtii CC-125
-
-
-
GPDH
-
-
GPDH-1
B4XU24
isozyme GPDH-1 is involved in the flight-muscle metabolism
GPDH-2
B4XU25
isozyme GPDH-2 provides precursors for lipid biosynthesis in many tissues
GPDH1
C5H3W0
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
GPDH1
Dunaliella viridis SHU
C5H3W0
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
-
GPDH2
C5H3W1
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
GPDH2
Dunaliella viridis SHU
C5H3W1
isozyme; isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains
-
GPDH: NAD+ 2 oxidorreductase
B4XU24, B4XU25
-
GPDHc1
O22216
-
hydroglycerophosphate dehydrogenase
-
-
-
-
L-alpha-glycerol phosphate dehydrogenase
-
-
-
-
L-alpha-glycerophosphate dehydrogenase
-
-
-
-
L-glycerol 3-phosphate dehydrogenase
-
-
L-glycerol phosphate dehydrogenase
-
-
-
-
L-glycerophosphate dehydrogenase
-
-
-
-
mGPDH
-
-
NAD+-dependent glycerol 3-phosphate dehydrogenase
-
-
NAD+-dependent glycerol-3-phosphate dehydrogenase
A8W1U0
-
NAD+-GPDH
Chlamydomonas reinhardtii CC-125
-
-
-
NAD-alpha-glycerophosphate dehydrogenase
-
-
-
-
NAD-dependent cG3PDH
-
-
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
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9075-65-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
honey bee
-
-
Manually annotated by BRENDA team
bumblebee species
-
-
Manually annotated by BRENDA team
strain Wiedemann, mediterranean fruit fly
-
-
Manually annotated by BRENDA team
Ceratitis capitata Wiedemann
strain Wiedemann, mediterranean fruit fly
-
-
Manually annotated by BRENDA team
strain 11/32-90, green alga
-
-
Manually annotated by BRENDA team
three GPDH genes, CrGPDH1, CrGPDH2, and CrGPDH3
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 11/32-90
strain 11/32-90, green alga
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CC-125
three GPDH genes, CrGPDH1, CrGPDH2, and CrGPDH3
-
-
Manually annotated by BRENDA team
japanese quail
-
-
Manually annotated by BRENDA team
from Southeastern Wyoming
-
-
Manually annotated by BRENDA team
van Rij strain 26, salt-tolerant
-
-
Manually annotated by BRENDA team
Debaryomyces nepalensis NCYC 3413
-
-
-
Manually annotated by BRENDA team
fruit fly, Samarkand wild-type
-
-
Manually annotated by BRENDA team
Dunaliella salina 435
-
-
-
Manually annotated by BRENDA team
; isozyme GPDH1; strain SHU
UniProt
Manually annotated by BRENDA team
; isozyme GPDH2; strain SHU
UniProt
Manually annotated by BRENDA team
Dunaliella viridis SHU
isozyme GPDH1; strain SHU
UniProt
Manually annotated by BRENDA team
Dunaliella viridis SHU
isozyme GPDH2; strain SHU
UniProt
Manually annotated by BRENDA team
; jerboa
-
-
Manually annotated by BRENDA team
strain Leishmania mexicana mexicana
-
-
Manually annotated by BRENDA team
new Zealand white
-
-
Manually annotated by BRENDA team
inbred Lewis strain euthyroid, hyperthyroid and hypothyroid male and female rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain Lou/C
-
-
Manually annotated by BRENDA team
Rattus norvegicus Lou/C
strain Lou/C
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
gene YDL022W encoding GPD1
SwissProt
Manually annotated by BRENDA team
isoforms Gdp1, Gut2
-
-
Manually annotated by BRENDA team
isoforms Gdp1p, Gdp2p
-
-
Manually annotated by BRENDA team
overexprssion of glycerol-3-phosphate dehydrogenase results in the production of more glycerol and less ethanol during fermentation
-
-
Manually annotated by BRENDA team
strain H44-3D
-
-
Manually annotated by BRENDA team
strain YSH 11-6B
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae H44-3D
strain H44-3D
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Y47
strain Y47
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YSH 11-6B
strain YSH 11-6B
-
-
Manually annotated by BRENDA team
spinach, cv Long Standing Bloomsdale
-
-
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
Manually annotated by BRENDA team
isozyme GPDH-1
UniProt
Manually annotated by BRENDA team
isozyme GPDH-2
UniProt
Manually annotated by BRENDA team
strain Trypanosoma brucei brucei
-
-
Manually annotated by BRENDA team
yellow jacket
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
Q00055
structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases, overview
malfunction
-
Drosophila GPDH-1-null mutants cannot fly
metabolism
Q00055
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
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 20C and 40C. 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
Q00055
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
Debaryomyces nepalensis NCYC 3413
-
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 20C and 40C. 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
Sus scrofa Duroc x Yorkshire x Landrace
-
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
-
metabolism
Dunaliella salina 435
-
glycerol-3-phosphate dehydrogenase is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate to glycerol-3-phosphate
-
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
Dunaliella salina 435
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
P21695
an electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analysis
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
show the reaction diagram
-
-
-
-
?
glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
show the reaction diagram
-
-
-
-
r
glycerone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
r
glycerone phosphate + NADH
L-glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
r
glycerone phosphate + NADH
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
-
-
-
-
r
glycolaldehyde + NADH
?
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
C5H3W0, C5H3W1
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
B4XU24, B4XU25
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
reverse reaction favoured direction
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
favoured reaction of heart isozyme II6.1
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
C5H3W0, C5H3W1
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+
show the reaction diagram
Ceratitis capitata Wiedemann
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Dunaliella viridis SHU
C5H3W0, C5H3W1
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Dunaliella viridis SHU
C5H3W0, C5H3W1
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+
show the reaction diagram
Rattus norvegicus Lou/C
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Saccharomyces cerevisiae H44-3D
-
-, oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Saccharomyces cerevisiae YSH 11-6B
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Chlamydomonas reinhardtii 11/32-90
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
D2XN65, -
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Q00055
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Dunaliella salina 435
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Chlamydomonas reinhardtii CC-125
-
-
-
-
r
sn-glycerol 3-phosphate + NADP+
dihydroxyacetone phosphate + NADPH + H+
show the reaction diagram
C5H3W0, C5H3W1
-
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+
show the reaction diagram
C5H3W0, C5H3W1
-
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+
show the reaction diagram
Dunaliella viridis SHU
C5H3W0, C5H3W1
-
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+
show the reaction diagram
Dunaliella viridis SHU
C5H3W0, C5H3W1
-
the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH
-
?
sn-glycerol 3-phosphate + NAPD+
dihydroxyacetone phosphate + NADPH + H+
show the reaction diagram
C5H3W0, C5H3W1
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 + NAPD+
dihydroxyacetone phosphate + NADPH + H+
show the reaction diagram
Dunaliella viridis SHU
C5H3W0, C5H3W1
isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme
-
-
?
L-glycerol-3-phosphate + NAD+
glycerone phosphate + NADH
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
glycerol
-
-
-
additional information
?
-
-
glycerol
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
glyceraldehyde-3-phosphate
-
-
-
additional information
?
-
-
DL-glyceraldehyde, phosphohydroxypyruvate
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
fructose-6-phosphate, fructose-1,6-bisphosphate
-
-
-
additional information
?
-
-
glucose-6-phosphate, acetaldehyde, oxaloacetate, no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
additional information
?
-
-
no substrates: dihydroxyacetone
-
-
-
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 DhGPD1 (glycerol 3-phosphate dehydrogenase) and DhGPP2 (glycerol 3-phosphatase)
-
-
-
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
?
-
-
involved in cellular acidosis, oxidoresistance, apoptosis by both acidosis and cell-cell contact inhibition, cell growth, and the generation of recombinant proteins
-
-
-
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
?
-
Saccharomyces cerevisiae H44-3D
-
glycerol, no substrates: dihydroxyacetone
-
-
-
additional information
?
-
Chlamydomonas reinhardtii 11/32-90
-
glyceraldehyde-3-phosphate, fructose-6-phosphate, fructose-1,6-bisphosphate, glucose-6-phosphate, acetaldehyde, oxaloacetate, no substrates: dihydroxyacetone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 25% the rate of dihydroxyacetone phosphate reduction at optimal pH
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
reverse reaction favoured direction
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
equilibrium far to the side of alpha-glycerophosphate at neutral pH
-
-
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
favoured reaction of heart isozyme II6.1
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
-
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+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
D2XN65, -
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Q00055
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Ceratitis capitata Wiedemann
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Saccharomyces cerevisiae H44-3D
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Dunaliella salina 435
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
show the reaction diagram
Chlamydomonas reinhardtii CC-125
-
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
show the reaction diagram
Saccharomyces cerevisiae YSH 11-6B
-
-
-
-
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
-
-
-
-
?
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 DhGPD1 (glycerol 3-phosphate dehydrogenase) and DhGPP2 (glycerol 3-phosphatase)
-
-
-
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
?
-
-
involved in cellular acidosis, oxidoresistance, apoptosis by both acidosis and cell-cell contact inhibition, cell growth, and the generation of recombinant proteins
-
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
B4XU24, B4XU25
;
NAD+
D2XN65, -
-
NAD+
Q00055
dependent on
NAD+
-
dependent on
NADH
-
1 mol per mol enzyme
NADH
-
2 mol per mol enzyme
NADH
-
2 mol per mol enzyme; spectrophoto-/fluorimetric monitoring
NADH
-
2 mol per mol enzyme
NADH
C5H3W0, C5H3W1
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
NADH
D2XN65, -
-
NADH
Q00055
dependent on
additional information
-
-
-
additional information
-
deamino-NAD+ 60.3% as effective as NAD+
-
additional information
-
3-acetylpyridine-NAD+ 1.5% as effective as NAD+; deamino-NAD+ 68% as effective as NAD+
-
additional information
-
no activity with NADPH
-
additional information
-
no activity with NADPH; not NADP+
-
additional information
-
no activity with NADPH; not NADP+
-
additional information
-
no activity with NADPH
-
additional information
-
activity with dihydroxyacetone phosphate and NADPH 5% of that with NADH
-
additional information
-
no activity with NADPH
-
additional information
-
no activity with NADPH
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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
MgCl2
-
0.1-0.3 M
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin-3-gallate
-
noncompetitive
(NH4)2SO4
-
-
(NH4)2SO4
-
inhibition of chloroplastic and cytosolic form
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
-
trypanocidal drug, IC50 0.00055 mM
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
-
IC50 0.0011 mM
3-morpholinosydnonimine
-
-
adenosine diphosphate ribose
-
0.094 mM slightly inhibits NADH binding by honeybee GPDH, but not by rabbit GPDH
adenosine diphosphate ribose
-
-
ADP
-
at physiological concentration, 10 mM 90% inhibition
ADP-ribose
-
allosteric inhibitor
ATP
-
at physiological concentration, 10 mM 95% inhibition
ATP
-
weak inhibitor of both isozymes, i.e. GPDH-1 and -3
Cd2+
-
50% inhibition at 8.33 mM; 50% inhibition at 8.3 mM
Cl-
-
cations, i.e. H+, K+, Na+ associated with Cl- do not affect the reduction of dihydroxyacetone phosphate
Cl-
-
competitive inhibitor with respect to dihydroxyacetone phosphate
Cu2+
-
50% inhibition at 12.96 mM; 50% inhibition at 13.0 mM
dihydroxyacetone phosphate
-
high levels of substrate, i.e. dihydroxyacetone phosphate result in inhibition
dihydroxyacetone phosphate
-
0.5 mM, GPDHs more susceptible to inhibition
dihydroxyacetone phosphate
-
substrate inhibition above 1 mM, NADH above 0.2 mM; substrate inhibition only at high concentration, over 1 mM
dihydroxyacetone phosphate
-
substrate inhibition at 0.2 mM
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
gymnemic acid
-
may have some pharmacological activities including antidiabetic activity and lipid lowering effects via interaction with G3PDH
iodoacetamide
-
effective inhibitor
iodoacetate
-
-
iodoacetate
-
0.1 mM 23% inhibition
iodoacetate
-
reversible by dithiothreitol, 10 mM inhibits to 50%
iodoacetate
-
50 mM, incubated for 60 min
K+
-
50% inhibition at 40.66 mM; 50% inhibition at 40.7 mM
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
-
over 0.025 mM, strong inhibitor of cytosolic and chloroplastic enzyme
L-glycerol 3-phosphate
-
competitive inhibitor to dihydroxyacetone phosphate, non-competitive to NADH
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
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 complete inhibition
N-ethylmaleimide
-
-
N-ethylmaleimide
-
reversible by dithiothreitol, 5 mM inhibits more than 90% of the enzyme activity
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
NaCl
-
inactivates irreversibly
NaCl
-
inactivation
NaCl
-
strongly inhibits, 50% activity at 250 mM NaCl
NaCl
C5H3W0, C5H3W1
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
NAD+
-
competitive inhibitor to NADH at physiological concentration
NADH
-
at high concentration
NADH
-
at high concentration
NADH-X
-
allosteric inhibitor
NADPH
-
inhibits in presence of saturing concentration of NADH and dihydroxyacetone phosphate
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-chloromercuribenzoate
-
10 nM, strong inhibition; reversible by dithiothreitol, 0.001 mM inhibits more than 90% of the enzyme activity
p-chloromercuribenzoate
-
0.0001 mM inhibits enzyme over 60%
p-chloromercuribenzoate
-
0.05 mM, 100% inhibition
p-chloromercuribenzoate
-
10 nM, strong inhibition
p-chloromercuribenzoate
-
0.1 mM, reversed by thiols, e.g. dithiothreitol
p-chloromercuribenzoate
-
effective inhibitor
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
phosphate
-
competitive inhibition
phosphate
-
slight inhibition of cytosolic form, at higher concentrations above 20-30 mM both forms are inhibited
phosphate
-
competitive inhibitor against dihydroxyacetone phosphate, non-competitive inhibitor against NADH
phosphate
C5H3W0, C5H3W1
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
phosphatidyl choline
-
0.003 mM, 42% inhibition of chloroplastic form and 43% inhibition of cytosolic form
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
suramin
-
trypanocidal drug, potent inhibitor, IC50 0.0002 mM
suramin
-
IC50 0.00044 mM
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
Mn2+
-
50% inhibition at 36.6 mM
additional information
-
no inhibition by NADPH, acetaldehyde, glycerol, ethanol
-
additional information
-
coenzyme analogs: acetylpyridine-NAD+, deaminoacetylpyridine-NAD+, pyridinealdehyde-NAD+, deaminopyridinealdehyde-NAD+, potent inhibitors
-
additional information
-
high ionic strength above 0.03 M
-
additional information
-
-
-
additional information
-
cyclic-AMP
-
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
C5H3W0, C5H3W1
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
-
the hyperthyroid status leads to a significant decrease of both enzyme amount and activity in both female and male animals
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
slight activation
Bovine serum albumin
-
activity increased
-
Dihydrolipoic acid
-
stimulation of chloroplastic form, 147% of enzyme activity
dipotassium malate
-
slight activation at low ionic strength
dithiothreitol
-
stimulation of chloroplastic form, 150% of enzyme activity
EDTA
-
without EDTA the rates are about 60% of the maximal rate
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
phosphate
-
around 5 mM, activation, chloroplastic form
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
phosphogluconate
-
0.005 mM slightly stimulates chloroplastic form
potassium glutamate
-
up to 0.1 M, activation, high activity also at high ionic strength
Glycine buffer
-
0.9 M, slight activation
-
additional information
C5H3W0, C5H3W1
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.075
-
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
-
-
0.19
-
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
-
-
1.6
-
glycerol phosphate
-
-
0.468
-
glycerol-3-phosphate
-
pH 9.0, 25C
1.7
-
glycerol-3-phosphate
-
-
2.25
-
glycerol-3-phosphate
-
-
34
-
glycerol-3-phosphate
-
isoform Gut2, pH 6.8
0.137
-
Glycerone
-
pH 7.6, 25C
0.154
-
glycerone phosphate
-
pH 7.5, 5C, muscle isozyme
0.259
-
glycerone phosphate
-
pH 7.5, 5C, liver isozyme
0.26
-
glycerone phosphate
-
pH 7.5, 25C
0.279
-
glycerone phosphate
-
pH 7.5, 22C, muscle isozyme
0.352
-
glycerone phosphate
-
pH 7.5, 22C, liver isozyme
137
-
glycerone phosphate
-
pH 9.0, 25C
0.74
-
L-glycerol 3-phosphate
-
-
2.3
-
L-glycerol-3-phosphate
-
pH 10.0, 25C
0.0044
-
NAD+
-
adipose tissue
0.01
-
NAD+
-
muscle
0.036
-
NAD+
-
measured at pH 9.0
0.045
-
NAD+
-
pH 8.5, 22C, liver isozyme
0.09
-
NAD+
-
pH 8.5, 5C, liver isozyme
0.1003
-
NAD+
-
alpha-GPDHs, standard deviation 0.0041 mM
0.143
-
NAD+
-
pH 8.5, 22C, muscle isozyme
0.155
-
NAD+
-
pH 8.5, 5C, muscle isozyme
0.2
-
NAD+
-
pH 10.0, 25C
0.3
-
NAD+
-
standard deviation 0.06 mM
0.316
-
NAD+
-
pH 9.0, 25C
0.38
-
NAD+
-
GPDH-1
0.5
-
NAD+
-
-
0.65
-
NAD+
-
pH 7.5, 25C
316
-
NAD+
-
pH 7.6, 25C
0.001
-
NADH
-
pH 7.5, 22C, liver isozyme; pH 7.5, 5C, liver isozyme; pH 7.5, 5C, muscle isozyme
0.003
-
NADH
-
pH 7.5, 22C, muscle isozyme
0.0043
-
NADH
-
adipose tissue
0.005
-
NADH
-
measured at pH 7.5
0.005
-
NADH
-
pH 7.5, 25C
0.00526
-
NADH
-
alpha-GPDHs
0.006
-
NADH
-
-
0.0066
-
NADH
-
standard deviation 0.003 mM
0.01
-
NADH
-
muscle
0.01
-
NADH
-
less than 0.01 mM
0.01
-
NADH
-
less than 0.01 mM
0.032
-
NADH
-
pH 7.6, 25C
0.0589
-
NADH
C5H3W0, C5H3W1
recombinant isozyme GDH2
0.0592
-
NADH
C5H3W0, C5H3W1
isozyme GPDH2
0.078
-
NADH
-
GPDH-1
0.0905
-
NADH
C5H3W0, C5H3W1
isozyme GPDH1; recombinant isozyme GDH1
32.4
-
NADH
-
pH 9.0, 25C
0.0589
-
NADPH
C5H3W0, C5H3W1
isozyme GPDH1
0.0592
-
NADPH
C5H3W0, C5H3W1
recombinant isozyme GDH1
0.0726
-
NADPH
C5H3W0, C5H3W1
isozyme GPDH2; recombinant isozyme GDH2
469
-
sn-glycerol 3-phosphate
-
pH 7.6, 25C
0.143
-
sn-glycerol-3-phosphate
-
measured at pH 9.0
0.3
-
alpha-glycerol phosphate
-
-
additional information
-
alpha-glycerophosphate
-
Km values from five different isoelectric focused components
3.9
-
L-glycerol-3-phosphate
-
pH 7.5, 25C
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
188
-
dihydroxyacetone phosphate
-
per subunit of 33500 Da
345
-
dihydroxyacetone phosphate
-
reduction of synthetic dihydroxyacetone phosphate, 20C, pH 7, rabbit muscle
390
-
dihydroxyacetone phosphate
-
reduction of synthetic dihydroxyacetone phosphate, 20C, pH 7, rabbit muscle, under conditions where competitive inhibition by fructose 1,6-diphosphate are not excluded
19000
-
glycerone phosphate
-
pH 7.5, 25C
32
-
L-glycerol-3-phosphate
-
per subunit of 33500 Da
51
-
L-glycerol-3-phosphate
-
pH 7.5, 25C
78
-
L-glycerol-3-phosphate
-
pH 10.0, 25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
(-)-epigallocatechin-3-gallate
-
substrate dihydroxyacetone phosphate, pH 7.4, 25C; substrate NADH, pH 7.4, 25C
0.2
-
gymnemic acid
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
(-)-epigallocatechin-3-gallate
-
pH 7.4, 25C
0.00055
-
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
-
trypanocidal drug, IC50 0.00055 mM
0.0011
-
2-hydroxy-1,2,3-nonadecanetricarboxylic acid
-
IC50 0.0011 mM
0.0015
0.005
Melarsen oxide
-
cymelarsen, IC50 0.0015-0.005 mM
0.0002
-
suramin
-
trypanocidal drug, potent inhibitor, IC50 0.0002 mM
0.00044
-
suramin
-
IC50 0.00044 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.1
-
-
standard deviation 0.2, crude preparation, testes
33
-
-
isozyme P-V, liver
53.6
-
-
pH 7.6, 25C
55.6
-
-
pH 9.0, 25C
70.7
-
-
standard deviation 5.1, crude preparation, liver
77
-
-
isozyme I6.5, after affinity chromatography, after preparative isoelectric-focusing: 175 units/mg
80
-
-
estimated
88.2
-
-
-
96
-
-
isozyme P-I, liver
119
-
-
62 units/mg calculated by using protein concentration determined by dry-weight measurements
120
-
-
pH 7.5, 25C
123
-
-
isozyme P-IV, liver
156
-
-
isozyme GPDH-3
162
-
-
isozyme I5.9
170
-
-
standard deviation 45 units/mg
179.8
-
-
isozyme GPDH-1
180
-
-
mammary gland
234
-
-
adipose tissue,147 units/mg refer to protein determination by Kjeldahl nitrogen analysis
250
-
-
-
253
-
-
isozyme P-II, liver
257
-
-
purified enzyme, from liver, pH 8.5, 25C
282
-
-
purified enzyme, from muscle, pH 8.5, 25C
310
-
-
-
806
-
-
isozyme P-III, liver
2396
-
-
isoform Gut2, pH 6.8
additional information
-
-
activities with the different isozymes at different temperatures, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
glycerol-3-phosphate formation
6.6
-
-
broad pH optimum around pH 6.6
6.6
-
-
optimum pH for NADH oxidation around pH 6.6
6.8
-
-
reduction of dihydroxyacetone-P
6.8
-
-
reduction of dihydroxyacetone-P, isozyme GPDH-1
6.8
-
-
dihydroxyacetone phosphate reduction
6.8
-
-
most active
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
7.4
-
-
reduction of dihydroxyacetone-phosphate, isozyme GPDH-3
7.5
-
-
reduction of dihydroxyacetone phosphate, in 0.2 M phosphate buffer
7.5
-
-
dihydroxyacetone phosphate reduction
7.5
-
-
assay at, reduction reaction
7.6
-
-
maximum rate of dihydroxyacetone phosphate reduction
7.7
-
-
reduction of dihydroxyacetone phosphate; reduction reaction
8.5
-
-
assay at, oxidation reaction
9
-
-
glycerol-3-phosphate oxidation
9
-
-
oxidation of sn-glycerol-3-phosphate; oxidation reaction
9.3
-
-
liver, component P-III, pH optimum of testis enzyme also around pH 9.3
9.3
-
-
glycerol-phosphate oxidation
9.5
-
-
oxidation of glycerol-phosphate
9.6
-
-
dihydroxyacetone phosphate formation
10
-
-
optimum pH for NAD+ reduction about pH 10.0
10.2
-
-
oxidation of glycerol 3-phosphate, in 0.03 glycine buffer
additional information
-
-
optimum pH values for components P-I, P-II, PIV, P-V range between pH 8.2 and 8.6, liver
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7.5
-
highest activity, glycerol-3-phosphate formation
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
6.8
7.2
-
activity falls off rapidly as pH is increased
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
7.9
8.2
-
maximum activity in pH interval 7.9-8.2
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
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
isozymes P-I, P-V, liver
25
-
-
assay at
30
-
-
isozyme GPDHf, activity falls off at temperature above 30C
35
-
-
isozymes P-II, P-III, P-IV, liver
35
-
-
; oxidation of sn-glycerol-3-phosphate
40
-
-
isozyme GPDHm and GPDHs
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
highest activity observed
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Dunaliella salina 435
-
-
-
Manually annotated by BRENDA team
D2XN65, -
; 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
Manually annotated by BRENDA team
D2XN65, -
very low expression level
Manually annotated by BRENDA team
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
Manually annotated by BRENDA team
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
Manually annotated by BRENDA team
D2XN65, -
high expression level
Manually annotated by BRENDA team
D2XN65, -
higher expression level
Manually annotated by BRENDA team
-
adipofibroblast, embryonic cell culture, up to 10fold increase of activity in presence of chicken serum, further increase in presence of embryonic chicken serum
Manually annotated by BRENDA team
B4XU24, B4XU25
adult gonad; adult gonad
Manually annotated by BRENDA team
D2XN65, -
very low expression level
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
very low expression level
-
Manually annotated by BRENDA team
D2XN65, -
-
Manually annotated by BRENDA team
D2XN65, -
very low expression level
Manually annotated by BRENDA team
D2XN65, -
-
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
Manually annotated by BRENDA team
-
late third instar
Manually annotated by BRENDA team
B4XU24, B4XU25
fifth instar nymph; fifth instar nymph
Manually annotated by BRENDA team
-
also other blood components
Manually annotated by BRENDA team
-
about 60% of activity of adipose tissue
Manually annotated by BRENDA team
-
mRNA levels of glycerol-3-phosphate dehydrogenase increase during winter season reaching the maximum in mid-december
Manually annotated by BRENDA team
D2XN65, -
-
Manually annotated by BRENDA team
Rattus norvegicus Lou/C, Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
Manually annotated by BRENDA team
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
Manually annotated by BRENDA team
D2XN65, -
and cerebellum, 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 dorsi muscle and postnatal day 14 in cerebrum. Weaning decreases the expression level of the GPD1 gene
Manually annotated by BRENDA team
-
bovine smooth muscles
Manually annotated by BRENDA team
-
skeletal-muscle
Manually annotated by BRENDA team
-
thoracic flight muscle
Manually annotated by BRENDA team
-
thoracic flight muscle
Manually annotated by BRENDA team
-
breast muscle
Manually annotated by BRENDA team
-
thoracic flight muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
B4XU24, B4XU25
isozyme GPDH-2 is expressed more abundantly in female adult thoracic muscles than in those from males; thoracic muscle
Manually annotated by BRENDA team
D2XN65, -
-
Manually annotated by BRENDA team
D2XN65, -
very low expression level
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
very low expression level
-
Manually annotated by BRENDA team
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
Manually annotated by BRENDA team
-
mGPDH abundance and activity is significantly elevated in prostate cancer cell lines when compared to the normal prostate epithelial cell line PNT1A
Manually annotated by BRENDA team
-
Crocker sarcoma
Manually annotated by BRENDA team
-
about 10% of activity of adipose tissue
Manually annotated by BRENDA team
-
hibernator muscle, muscle isozyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
D2XN65, -
very low expression level
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
very low expression level
-
Manually annotated by BRENDA team
-
in adult worms on tegument urface, and in metacercaria on tegument and tegumentary cells
Manually annotated by BRENDA team
additional information
D2XN65, -
porcine GPD1 gene is expressed in almost all tissues but its levels of expression vary widely over 2 orders of magnitude
Manually annotated by BRENDA team
additional information
-
in adult worms noactivity in tissues, such as oral sucker, pharynx, esophagus, ventral sucker, and intrauterine eggs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Chlamydomonas reinhardtii 11/32-90
-
stroma, soluble
-
Manually annotated by BRENDA team
Dunaliella viridis SHU
-
;
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CC-125, Rattus norvegicus Lou/C
-
-
-
Manually annotated by BRENDA team
-
isoform Gpd2p, partly isoform Gpd1p
Manually annotated by BRENDA team
O22216
loss of GPDHc1 affects mitochondrial respiration, particularly through a diminished capacity of the alternative oxidase respiration pathway
Manually annotated by BRENDA team
Sus scrofa Duroc x Yorkshire x Landrace
-
-
-
Manually annotated by BRENDA team
-
determined by isopycnic gradient centrifugation
Manually annotated by BRENDA team
-
isoform Gpd2p, contains mitochondrial presequence sufficient for targeting
Manually annotated by BRENDA team
-
sn-glycerol 3-phosphate dehydrogenase generates superoxide about equally to each side of the membrane
Manually annotated by BRENDA team
-
localisation shown in Saccharomyces cerevisiae via GFP-fusion proteins
Manually annotated by BRENDA team
-
predicted from sequence
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
SDS-PAGE
59500
-
-
gel filtration
62000
-
-
gel filtration
63500
-
-
gel filtration
65000
-
-
gel filtration
66000
-
-
61000-71000 Da, gel filtration
66000
-
-
gel filtration
67000
-
-
gel filtration
68000
-
-
gel filtration
69000
-
-
66000-72000 Da, gel filtration
72000
-
-
gel filtration
72000
-
-
gel filtration; PAGE
72500
-
-
69000-76000, gel filtration
73000
-
-
calculated by amino acid analysis
74000
-
-
electrophoresis in a non-denaturing system
75000
-
-
calculated from subunit molecular weight and physical plus chemical properties
75000
-
-
sucrose density gradient ultracentrifugation
76000
-
-
meniscus depletion method
76000
-
-
gel filtration
76200
-
C5H3W0, C5H3W1
calculated from amino acid sequence
76500
-
-
74000-79000 Da, SDS-PAGE under non-denaturing conditions
77000
-
-
gel filtration
77200
-
C5H3W0, C5H3W1
calculated from amino acid sequence
78000
-
-
calculated from partial specific volume, sedimentation and diffusion data
78000
-
-
gel filtration
78600
-
-
fluorometric titrations
79500
-
-
meniscus depletion method
additional information
-
-
amino acid analysis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37500, isozyme from heart (II6.1), calculated by amino acid composition
?
-
x * 31000, gel filtration, estimated from elution volume on sepharose 6B
?
-
x * 33000, calculated from Stokes radius
?
-
x * 42000, SDS-PAGE
?
-
x * 37000, SDS-PAGE
?
-
x * 39140, calculated by cDNA-sequence
?
-
x * 37651, calculated by cDNA-sequence
?
-
x * 43000-47000, SDS-PAGE
?
A8W1U0, -
x * 42695, calculated from sequence
?
D2XN65, -
x * 37742, calculated
?
A5Z0R9, -
x * 40451, calculated
?
-
x * 42400, recombinant enzyme, SDS-PAGE
?
Chlamydomonas reinhardtii 11/32-90
-
x * 33000, calculated from Stokes radius
-
?
Saccharomyces cerevisiae YSH 11-6B
-
x * 43000-47000, SDS-PAGE
-
dimer
-
2 * 37200-37900
dimer
-
2 * 42000, SDS-PAGE
dimer
-
determined after carboxypeptidase A digestion
dimer
-
2 * 37500, gel filtration in 6 M guanidinium chloride, confirmed by amino acid composition
dimer
-
2 * 39000, gel filtration in guanidinium chloride
dimer
-
2 * 31700, SDS-PAGE
dimer
-
2 * 33500, SDS-PAGE
dimer
-
2 * 37000, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE, confirmed by amino acid composition
dimer
-
2 * 35000-37000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 35700, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
Ceratitis capitata Wiedemann
-
2 * 33500, SDS-PAGE
-
dimer
Saccharomyces cerevisiae H44-3D
-
2 * 42000, SDS-PAGE
-
additional information
-
37800-39300, rabbit muscle, minimal molecular weight calculated by titration with NADH at pH 6.0
additional information
-
kinetic interaction between NADH dehydrogenases Nde1/Nde2 and enzyme isoform Gut2 at inner mitochondrial membrane
additional information
Q00055
the enzyme monomer is organized with N- and C-terminal domains. The N-terminal domain contains a classic Rossmann fold with the (beta-alpha-beta-alpha-beta)2 motif typical of many NAD+-dependent enzymes, while the C-terminal domain is mainly alpha-helical, structure comparisons, overview
additional information
-
each one of the three CrGPDHs has a bi-domain protein structure: a GPDH domain of about 350 amino acids located at the C terminus, and a phosphoserine phosphatase (SerB) domain of about 200 amino acids at the N terminus. The GPDH domain of all three CrGPDHs contains the conserved GSGAWA motif at residues 261-266 (CrGPDH1), 316-321 (CrGPDH2), and 267-272 (CrGPDH3), three-dimensional structures by homology modeling, based on the Homo sapiens GPD1 crystal structure, overview
additional information
Chlamydomonas reinhardtii CC-125
-
each one of the three CrGPDHs has a bi-domain protein structure: a GPDH domain of about 350 amino acids located at the C terminus, and a phosphoserine phosphatase (SerB) domain of about 200 amino acids at the N terminus. The GPDH domain of all three CrGPDHs contains the conserved GSGAWA motif at residues 261-266 (CrGPDH1), 316-321 (CrGPDH2), and 267-272 (CrGPDH3), three-dimensional structures by homology modeling, based on the Homo sapiens GPD1 crystal structure, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
modification of Cys345 in hydrophobic pocket
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified GlpD is concentrated to 8 mg/ml and crystallized at 4C from a solution containing 0.1 M diammonium hydrogen phosphate, 0.1 M Bicine pH 8.5, and 12% w/v PEG 6000. Structure of the native enzyme, structures of enzyme complexed with substrate analogues phosphoenolpyruvate, glyceric acid 2-phosphate, glyceraldehyde-3-phosphate, and product, dihydroxyacetone phosphate
-
hanging-drop vapor-diffusion method enzyme/NAD+ complex, enzyme/dihydroxyacetonephosphate complex, enzyme/NAD+/dihydroxyacetonephosphate complex
P21695
purified recombinant untagged enzyme, hanging drop vapour diffusion method using a reservoir solution consisting of 12% PEG 8000, 0.1 M Tris-HCl, pH 8.5, 0.3 M MgCl2, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement and modeling
Q00055
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
9.9
-
stable at 21C for 15 min; stable for 15 min at 21C
5
9
-
under diluted conditions
5
-
-
inactivation after 1 h at 20C
5.7
8.5
-
around this range, most stable
6
9
-
stable for 16 h at 20C
7
-
-
less stable
7
-
-
rate of inactivation increases below pH 7
7
-
-
stable, increasing from 7.0 to 8.0 causes 80% loss of activity
10
-
-
inactivation after 1 h at 20C
additional information
-
-
more stable at alkaline pH, more stable in phosphate buffer than in Tris-glycine buffer
additional information
-
-
increasing pH from 7.0 to 8.0 causes 80% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
stable for at least 30 min
20
-
-
between pH 6.0 and 9.0, stable for 1 h
21
-
-
15 min stable; stable at pH 4.8-9.9 for 15 min
30
-
-
30 min stable, pH 6.6
35
-
-
most stable at pH 8, activity reduced, GPDHf to a greater extent
45
-
-
at least 5 min stable
45
-
-
pH 6.6, 5 min stable
48
-
-
t1/2: 15 min, muscle isozyme I6.5; t1/2: 2 min, brain isozyme I5.9; t1/2: 2 min, heart isozyme II6.1
48
-
-
t1/2: 2 min, brain isozyme I5.9; t1/2: 7.5 min, isozyme I6.5
50
-
-
rapid denaturation, prevented by 0.1 mg/ml bovine serum albumin, by over 20% ammonium sulfate or by 0.1 M phosphate buffer, pH 7.5
50
-
-
crude extract at least 20 min stable
50
-
-
t1/2: 2 min in heart and 10 min in muscle, mammary gland and liver
55
-
-
t1/2: 1 min
55
-
-
5 min stable in Tris-buffer plus EDTA and bovine serum albumin
55
-
-
inactivation after 30 min
60
-
-
complete inactivation after 1 min
60
-
-
inactivation after 5 min
60
-
-
inactivation after 5 min
61
-
-
complete inactivation after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol stabilizes
-
EDTA stabilizes
-
2-mercaptoethanol stabilizes during purification
-
2-mercaptoethanol does not stabilize
-
20% polyethylene glycol stabilizes during purification
-
dithiothreitol does not stabilize
-
EDTA stabilizes
-
20% polyethylene glycol stabilizes during purification
-
substrates stabilize dilute preparation
-
dithiothreitol stabilizes
-
EDTA stabilizes
-
NAD+ stabilizes
-
NADH stabilizes
-
phenylmethane-sulfonyl fluoride stabilizes during purification
-
2-mercaptoethanol stabilizes during purification
-
ammonium sulfate stabilizes
-
NADH stabilizes preparations of low ionic strength
-
ammonium sulfate inactivates
-
charcoal inactivates rabbit enzyme, restorable by thiamic acid
-
EDTA stabilizes
-
even cold dilute solutions in 0.2 M ammonium sulfate at pH 5.8 are stable for weeks
-
redistilled water prevents denaturation in absence of salts
-
2-mercaptoethanol stabilizes during purification
-
ammonium sulfate stabilizes
-
bovine serum albumin stabilizes
-
lyophilization inactivates
-
phosphate buffer stabilizes
-
repeated freezing and thawing results in rapid loss of activity, to some extent restorable at room temperature
-
the enzyme displays rapid induction as well as decay upon dissappearance of a hormonal stimulus (thyroid hormone), indicating a rather short half-life of the enzyme
-
freezing inactivates completely, ammonium sulfate prevents inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2C, crystals stable at least a month in 0.1 M Tris buffer, pH 7.6 with added EDTA, dithiothreitol and ammonium sulfate
-
crystals, 2C in 0.1M Tris, 10 mM EDTA, 2 mM dithiothreitol, pH 7.6, (NH4)2SO4 in final concentration of 1.7 M
-
-20C, stable for at least 2 months
-
0C, t1/2: 50 min
-
4C, 20% v/v, glycerol, purified stable
-
4C, t1/2: 6 h in absence of EDTA and polyethyleneglycol
-
0C, 30 mM Tris-H2SO4, 2.5 mM Na2EDTA, 5 mM dithiothreitol, 0,05% NaN3 (pH 8, 4C), 0.1 mM phenylmethylsulfonylfluoride, 15-17.5% w/v poly(ethylene glycol) 4000, after six days loss of activity insignificant
-
0C, crude extract stable for 6 days in presence of polyethylene glycol
-
5C, isozyme 1: stable for over a month in 10 mM sodium phosphate buffer, pH 6.5, with added EDTA, dithiothreitol and NADH, isozyme 3: 50% loss of activity under the same conditions
-
crystallized, in ammonium sulfate stable for months
-
-20C, 50% glycerol, retains activity for several months
-
4C, 20% v/v, glycerol, purified stable
-
4C, dilute solution, pH 5.8, stable for weeks
-
-20-0C, stable in 75% ammonium sulfate
-
-20C, in 0.1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, 50% polyethylene glycol 2000, 5 mM NADH or dihydroxyacetone phosphate, unstable
-
-80C, in 0.1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, 50% polyethylene glycol 2000, 5 mM NADH or dihydroxyacetone phosphate, unstable
-
4C, 1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, eluted from Sephadex G-100 column, 90% activity remained after several weeks
-
4C, stable for several weeks in 1 M Tris/HCl buffer with 2-mercaptoethanol, pH 7.0
-
-20C, stable as (NH4)2SO4-precipitate
-
4C, purified and dilute preparation stable for several days in presence of NADH
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
6 to 8 isozymes of bumblebee flight muscle enzyme
-
dye-affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
4 isozymes in testes and 5 isozymes in liver, distinct in isoelectric focusing
-
native enzyme 50fold and 176fold from liver and muscle, respectively, by anion exchange chromatography, gel filtration, and affinity chromatography
-
2 allelic forms of the enzyme; affinity chromatography
-
3 isozymes in adults and 1 in larvae, distinct in isoelectric focusing; affinity chromatography
-
3 isozymes, product of the same gene mapped to left arm of chromosome II, isozyme 1: flight muscle, isozyme 3: larval and adult fat body, isozyme 2: heterodimer of 1 and 3; affinity chromatography
-
3 allelic forms distinguishable by electrophoresis
-
GSTrap column chromatography; GSTrap column chromatography
C5H3W0, C5H3W1
-
P21695
affinity chromatography
-
2 isozymes with distinct isoelectric points in brain
-
preparative isoelectric focusing
-
sequential affinity chromatography; several isozymes, distinct in isoelectric points
-
several isozymes, distinct in isoelectric points
-
ion-exchange chromatography combined with affinity elution, 2 isozymes that differ in charge by analytical PAGE
-
affinity chromatography
-
recombinant enzyme from Escherichia coli strain BL21 by anion exchange chromatography to over 95% purity
Q00055
2 isozymes
-
affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli with the maltose-binding protein fusion system
-
genes CrGPDH1, CrGPDH2, and CrGPDH3, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Saccharomyces cerevisiae. Although the gene is functional in Saccharomyces cerevisiae, its heterologous expression is not efficient, suggesting that the regulatory mechanism may not be shared by Debaryomyces hansenii and Saccharomyces cerevisiae
-
expressed in Escherichia coli BL21(DE3) pLysScells; expressed in Escherichia coli BL21(DE3) pLysScells; expressed in Escherichia coli BL21(DE3) pLysS cells; expressed in Escherichia coli BL21(DE3) pLysS cells
C5H3W0, C5H3W1
expression in CHO cells
-
expression in Escherichia coli BL-21 DE3 as a fusion protein with glutathione S-transferase
P21695
expression in Saccharomyces cerevisiae
-
recombinant in Escherichia coli
-
gene YDL022W, phylogenetic analysis, expression in Escherichia coli strain BL21
Q00055
GPD1, phylogenetic analysis, relative quantitative real-time PCR, expression of GFP-tagged GPD1 in PK-15 cells
D2XN65, -
recombinant in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
effects of salinity changes on the gene expressions of a (NAD+)-dependent G3pdh among G3pdh isozymes by real-time quantitative PCR, overview. Expression level of G3pdh in Dunaliella salina grown at various salinities is significantly inversely correlated to the salinity, but there is no significant correlation between the expression level of G3pdh and salinity after 2 h of treatment by hyperosmotic or hypoosmotic shock
-
effects of salinity changes on the gene expressions of a (NAD+)-dependent G3pdh among G3pdh isozymes by real-time quantitative PCR, overview. Expression level of G3pdh in Dunaliella salina grown at various salinities is significantly inversely correlated to the salinity, but there is no significant correlation between the expression level of G3pdh and salinity after 2 h of treatment by hyperosmotic or hypoosmotic shock
Dunaliella salina 435
-
-
gene expression level is high after 2 h induction in a hyperosmotic environment containing 2 M NaCl and returns to normal within 6 h
A5Z0R9, -
porcine GPD1 gene is expressed in almost all tissues but its levels of expression vary widely over 2 orders of magnitude. Longissinus doris muscle and cerebrum have a 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
D2XN65, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Deltagpd1
-
anaerobic growth, growth rate and glycerol production similar to wild-type
Deltagpd1/Deltacox18
-
anaerobic growth, growth rate and glycerol production similar to wild-type
Deltagpd2
-
50% decrease in anaerobic glycerol production
Deltagpd2/Deltacox18
-
no growth under anaerobic or aerobic conditions
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
green tea catechin (-)-epigallocatechin-3-gallate is a noncompetitive inhibitor of glycerol-3-phosphate dehydrogenase
medicine
-
the hyperthyroid status leads to a significant decrease and the hypothyroid status to a significant increase of both enzyme amount and activity in both female and male animals. The euthyroid and hyperthyroid females show a higher activity and the hyperthyroid females also show a higher enzyme amount in comparison with male animals, while the hypothyroid animals show low levels in both sexes. The enzyme-dependent oxygen consumption of freshly isolated liver mitochondria from hyperthyroid animals is higher compared with euthyroid animals, and is activated bycoenzyme Q analogue idebenone, in both euthyroid and hyperthyroid rats. Determination of enzyme amount and activity can serve as an additional criterion for the evaluation of the thyroid hormone status
biotechnology
-
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
nutrition
-
yeast strains overexpressing glycerol-3-phosphate dehydrogenase may be used to produce wine with decreased ethanol content
synthesis
-
fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway (strain with deletions in both genes encoding specific L-G3Pases (GPP1 and GPP2) and multicopy overexpression of L-glycerol 3-phosphate dehydrogenase). Up-scaling the process employs fed-batch fermentation with repeated glucose feeding, plus an aerobic growth phase followed by an anaerobic product accumulation phase. This produces a final product titer of about 325 mg total L-glycerol 3-phosphate per liter of fermentation broth
synthesis
-
successful introduction of a glycerol production pathway into Klebseiella pneumoniae by coexpression of genes encoding glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase (EC 3.1.3.21) organized into the plasmid pUC18K under control of the respective lac promoter. An engineered Klebsiella pneumoniae that can produce glycerol from glucose is achieved. It is still difficult to efficiently produce 1,3-propanediol from glucose. Only 0.58 g/l 1,3-propanediol is produced
synthesis
-
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
synthesis
Saccharomyces cerevisiae Y47
-
successful introduction of a glycerol production pathway into Klebseiella pneumoniae by coexpression of genes encoding glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase (EC 3.1.3.21) organized into the plasmid pUC18K under control of the respective lac promoter. An engineered Klebsiella pneumoniae that can produce glycerol from glucose is achieved. It is still difficult to efficiently produce 1,3-propanediol from glucose. Only 0.58 g/l 1,3-propanediol is produced
-