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(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
(2R,3R)-2,3-butanediol + NAD+
? + NADH
(R)-1,2-propanediol + NAD+
? + NADH
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH
1,2,3-butanetriol + NAD+
1,3-dihydroxybutane-2-one + NADH
-
-
-
?
1,2-butanediol + NAD+
1-hydroxy-2-butanone + NADH + H+
-
-
-
?
1,2-butanediol + NAD+
1-hydroxybutane-2-one + NADH
-
-
-
r
1,2-butanediol + NAD+
? + NADH
1,2-ethanediol + NAD+
hydroxyacetaldehyde + NADH + H+
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
1,3-butanediol + NAD+
?
-
relative activity is 6.5% compared to oxidation of glycerol
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
1,4-butanediol + NAD+
? + NADH + H+
1-butanol + NAD+
butanal + NADH + H+
1-chloro-2,3-propanediol + NAD+
?
1-octanol + NAD+
octanal + NADH + H+
1-phenylethan-1,2-diol + NAD+
? + NADH
-
-
-
-
?
1-phenylethanol + NAD+
acetophenone + NADH + H+
-
-
-
-
?
1-propanol + NAD+
propanal + NADH + H+
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
?
2-propanol + NAD+
acetone + NADH + H+
3-(2,2,2-trifluoroethoxy)propane-1,2-diol + NAD+
1-hydroxy-3-(2,2,2-trifluoroethoxy)propan-2-one + NADH + H+
-
-
-
?
3-(2,2,2-trifluoroethoxy)propane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-amino-1,2-propanediol + NAD+
?
-
104% of the activity with glycerol
-
-
?
3-bromo-1,2-propanediol + NAD+
?
-
109% of the activity with glycerol
-
-
?
3-butoxypropane-1,2-diol + NAD+
1-hydroxy-3-butoxypropan-2-one + NADH + H+
-
-
-
?
3-butoxypropane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-chloro-1,2-propanediol + NAD+
?
-
130% of the activity with glycerol
-
-
?
3-ethoxypropane-1,2-diol + NAD+
1-hydroxy-3-ethoxypropan-2-one + NADH + H+
-
-
-
?
3-ethoxypropane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-hydroxypropionaldehyde + NADH
propan-1,3-diol + NAD+
-
-
-
-
?
3-mercapto-1,2-propanediol + NAD+
?
-
155% of the activity with glycerol
-
-
?
3-methoxypropane-1,2-diol + NAD+
1-hydroxy-3-methoxypropan-2-one + NADH + H+
-
-
-
?
3-methoxypropane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-phenoxypropane-1,2-diol + NAD+
1-hydroxy-3-phenoxypropan-2-one + NADH + H+
-
-
-
?
3-phenoxypropane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-propoxypropane-1,2-diol + NAD+
1-hydroxy-3-propoxypropan-2-one + NADH + H+
-
-
-
?
3-propoxypropane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
3-[(propan-2-yl)oxy]propane-1,2-diol + NAD+
1-hydroxy-3-[(propan-2-yl)oxy]propan-2-one + NADH + H+
-
-
-
?
3-[(propan-2-yl)oxy]propane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
acetoin + NADH + H+
2,3-butanediol + NAD+
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
-
-
-
?
beta-glycerophosphate + NAD+
?
-
relative activity is 2% compared to oxidation of glycerol
-
-
?
butane-1,3-diol + NAD+
? + NADH
-
-
-
-
?
butane-2,3-diol + NAD+
? + NADH + H+
D-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
-
-
-
?
D-2,3-butanediol + NAD+
? + NADH + H+
-
-
-
?
D-glyceraldehyde + NADH + H+
glycerol + NAD+
-
-
-
-
r
diglycerol + NAD+
?
-
relative activity is 21% compared to oxidation of glycerol
-
-
?
dihydroxyacetone + NADH + H+
glycerol + NAD+
-
-
-
-
r
DL-alpha-glycerophosphate + NAD+
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
DL-glyceraldehyde + NADH
glycerol + NAD+
erythrite + NAD+
?
-
-
-
-
?
ethanediol + NAD+
glycolaldehyde + NADH
ethanol + NAD+
acetaldehyde + NADH
-
relative activity is 1% compared to oxidation of glycerol
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
ethylene glycol + NAD+
? + NADH + H+
glycerol + N6-carboxymethyl-NAD+
glycerone + N6-carboxymethyl-NADH + H+
glycerol + N6-CM-NAD+
glycerone + N6-carboxymethyl-NADH + H+
glycerol + NAD+
D-glyceraldehyde + NADH + H+
glycerol + NAD+
dihydroxyacetone + NADH + H+
glycerol + NAD+
glycerone + NADH + H+
glycerol + NADP+
dihydroxyacetone + NADPH + H+
glycerol + NADP+
glyceraldehyde + NADPH + H+
glycerol-alpha-monochlorohydrin + NAD+
?
glycerol-alpha-monomethyl ether + NAD+
?
glycerone + NADH + H+
glycerol + NAD+
hydroxy-2-propanone + NADH
propylene glycol + NAD+
-
relative activity is 27% compared to oxidation of glycerol
-
-
?
i-inositol + NAD+
?
-
relative activity is 18% compared to oxidation of glycerol
-
-
?
isopropanol + NAD+
acetone + NADH
-
relative activity is 17% compared to oxidation of glycerol
-
-
?
L-1,2-propanediol+ NAD+
hydroxyacetone + NADH + H+
-
-
-
?
L-2,3-butanediol + NAD+
? + NADH + H+
-
-
-
?
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH
methylglyoxal + NADH
lactaldehyde + NAD+
N-butyraldehyde + NADH
1-butanol + NAD+
-
-
-
-
?
propane-1,2-diol + NAD+
propane-1-ol-2-one + NADH
-
-
-
-
?
propionaldehyde + NADH
1-propanol + NAD+
-
-
-
-
?
pyruvate + NADH + H+
D-lactate + NADH
-
-
-
?
R-1-amino-2-propanol + NAD+
?
-
33% of the activity with glycerol
-
-
?
racemic 2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH + H+
S-1-amino-2-propanol + NAD+
?
-
9% of the activity with glycerol
-
-
?
sorbitol + NAD+
?
-
relative activity is 3% compared to oxidation of glycerol
-
-
?
additional information
?
-
(2R,3R)-2,3-butanediol + NAD+

(3R)-acetoin + NADH
-
-
more than 99% enantiomeric excess of R-product
-
r
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
more than 99% enantiomeric excess of R-product
-
r
(2R,3R)-2,3-butanediol + NAD+

? + NADH
-
better substrate than glycerol
-
-
?
(2R,3R)-2,3-butanediol + NAD+
? + NADH
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+

? + NADH
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+
? + NADH
-
better substrate than glycerol
-
-
?
(R)-1,2-propanediol + NAD+

hydroxyacetone + NADH
the enzyme prefers the R-enantiomer
-
-
r
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH
the enzyme prefers the R-enantiomer
-
-
r
1,2-butanediol + NAD+

? + NADH
-
-
-
?
1,2-butanediol + NAD+
? + NADH
-
-
-
?
1,2-propanediol + NAD+

hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
105% of the activity with glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
relative activity is 116% compared to oxidation of glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
r
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
relative activity is 116% compared to oxidation of glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
as active as glycerol
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
1,2-propanediol represses the global activator HilA that induces an invasive phenotype and repression of HilA could be weakened by glycerol dehydrogenase activity
-
-
?
1,2-propanediol + NAD+
hydroxyacetone + NADH
-
-
-
r
1,3-butanediol + NAD+

4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
-
?
1,3-butanediol + NAD+
4-hydroxy-2-butanone + NADH + H+
-
-
-
?
1,3-dichloro-2-propanol + NAD+

1,3-dichloro-2-propanone + NADH
-
-
-
-
?
1,3-dichloro-2-propanol + NAD+
1,3-dichloro-2-propanone + NADH
-
-
-
-
?
1,3-propanediol + NAD+

?
-
relative rate of oxidation is 18% compared to oxidation of glycerol
-
-
?
1,3-propanediol + NAD+
?
-
-
-
-
?
1,3-propanediol + NAD+
?
-
-
-
-
?
1,3-propanediol + NAD+
?
-
relative rate of oxidation is 37% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+

?
-
relative activity is 0.3% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+
?
-
relative activity 17% compared to oxidation of glycerol
-
-
?
1,4-butanediol + NAD+

? + NADH + H+
-
-
-
-
?
1,4-butanediol + NAD+
? + NADH + H+
-
-
-
?
1-butanol + NAD+

butanal + NADH + H+
-
-
-
-
?
1-butanol + NAD+
butanal + NADH + H+
-
-
-
-
?
1-chloro-2,3-propanediol + NAD+

?
-
-
-
-
?
1-chloro-2,3-propanediol + NAD+
?
-
-
-
-
?
1-octanol + NAD+

octanal + NADH + H+
-
-
-
-
?
1-octanol + NAD+
octanal + NADH + H+
-
-
-
-
?
1-propanol + NAD+

propanal + NADH + H+
-
-
-
-
?
1-propanol + NAD+
propanal + NADH + H+
-
-
-
-
?
2,3-butanediol + NAD+

3-hydroxybutane-2-one + NADH
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
r
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
r
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
as active as glycerol
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
-
-
-
r
2-propanol + NAD+

acetone + NADH + H+
-
-
-
-
?
2-propanol + NAD+
acetone + NADH + H+
-
-
-
-
?
acetaldehyde + NADH + H+

ethanol + NAD+
-
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
-
?
acetoin + NADH + H+

2,3-butanediol + NAD+
-
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
-
r
butane-2,3-diol + NAD+

? + NADH + H+
-
-
-
?
butane-2,3-diol + NAD+
? + NADH + H+
-
-
-
?
DL-alpha-glycerophosphate + NAD+

?
-
oxidation at 16% compared to oxidation of glycerol
-
-
?
DL-alpha-glycerophosphate + NAD+
?
-
relative activity 11%compared to oxidation of glycerol
-
-
?
DL-glyceraldehyde + NAD+

3-hydroxypyruvaldehyde + NADH
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
relative rate of reduction is 14%compared to reduction of dihydroxyacetone
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
-
-
-
?
DL-glyceraldehyde + NAD+
3-hydroxypyruvaldehyde + NADH
-
-
-
?
DL-glyceraldehyde + NADH

glycerol + NAD+
-
-
-
-
?
DL-glyceraldehyde + NADH
glycerol + NAD+
-
-
-
-
?
ethanediol + NAD+

glycolaldehyde + NADH
-
-
reduction at concentration of 50 mM
r
ethanediol + NAD+
glycolaldehyde + NADH
-
-
reduction at concentration of 50 mM
r
ethanediol + NAD+
glycolaldehyde + NADH
-
-
-
?
ethylene glycol + NAD+

?
-
-
-
-
?
ethylene glycol + NAD+
?
-
relative activity is 20% compared to oxidation of glycerol
-
-
?
ethylene glycol + NAD+
?
-
-
-
?
ethylene glycol + NAD+
?
-
-
-
?
ethylene glycol + NAD+

? + NADH + H+
-
-
-
?
ethylene glycol + NAD+
? + NADH + H+
-
-
-
?
ethylene glycol + NAD+
? + NADH + H+
-
-
-
-
?
glycerol + N6-carboxymethyl-NAD+

glycerone + N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + N6-carboxymethyl-NAD+
glycerone + N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + N6-CM-NAD+

glycerone + N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + N6-CM-NAD+
glycerone + N6-carboxymethyl-NADH + H+
-
-
-
r
glycerol + NAD+

D-glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
D-glyceraldehyde + NADH + H+
-
-
-
-
r
glycerol + NAD+
D-glyceraldehyde + NADH + H+
-
-
-
?
glycerol + NAD+
D-glyceraldehyde + NADH + H+
-
no activity with NADP+. The enzyme shows much higher activity towards glycerol as compared to short chain primary and secondary alcohols. The thermostable enzyme is highly stereospecific in oxidation of glycerol and converts glycerol into D-glyceraldehyde
-
-
r
glycerol + NAD+
D-glyceraldehyde + NADH + H+
-
no activity with NADP+. The enzyme shows much higher activity towards glycerol as compared to short chain primary and secondary alcohols. The thermostable enzyme is highly stereospecific in oxidation of glycerol and converts glycerol into D-glyceraldehyde
-
-
r
glycerol + NAD+

dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
Glycerol dehydrogenase was immobilised in a polycarbamoyl sulfonate-hydrogel to be used as a sensor for glycerol. Glycerol oxidation leads to the reduction of NAD+ to NADH and electrons are transferred to ferricyanide on an electrode surface
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
the enzyme exhibits an exclusive preference for NAD+ over NADP+
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
the enzyme exhibits an exclusive preference for NAD+ over NADP+
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
-
?
glycerol + NAD+

glycerone + NADH + H+
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH + H+
no activity detected with NADP+
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
glycerone reduction is the dominant reaction
i.e. 1,3-dihydroxypropranone
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
glycerone reduction is the dominant reaction
i.e. 1,3-dihydroxypropranone
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
-
-
?
glycerol + NADP+

dihydroxyacetone + NADPH + H+
the enzyme exhibits an exclusive preference for NAD+ over NADP+
-
-
?
glycerol + NADP+
dihydroxyacetone + NADPH + H+
the enzyme exhibits an exclusive preference for NAD+ over NADP+
-
-
?
glycerol + NADP+

glyceraldehyde + NADPH + H+
-
-
-
-
?
glycerol + NADP+
glyceraldehyde + NADPH + H+
-
activity observed with pentan-1-ol, 3-methyl-butan-1-ol, 1-decanol, low activity as ethanol dehydrogenase with NAD+ or NADPH+ as cofactor
-
-
?
glycerol + NADP+
glyceraldehyde + NADPH + H+
-
-
-
-
?
glycerol + NADP+
glyceraldehyde + NADPH + H+
-
activity observed with pentan-1-ol, 3-methyl-butan-1-ol, 1-decanol, low activity as ethanol dehydrogenase with NAD+ or NADPH+ as cofactor
-
-
?
glycerol-alpha-monochlorohydrin + NAD+

?
-
relative rate of oxidation is 71% compared to oxidation of glycerol
-
-
?
glycerol-alpha-monochlorohydrin + NAD+
?
-
relative rate of oxidation is 26% compared to oxidation of glycerol
-
-
?
glycerol-alpha-monomethyl ether + NAD+

?
-
-
-
-
?
glycerol-alpha-monomethyl ether + NAD+
?
-
-
-
-
?
glycerone + NADH + H+

glycerol + NAD+
-
-
-
-
r
glycerone + NADH + H+
glycerol + NAD+
-
-
-
-
r
meso-2,3-butanediol + NAD+

(3S)-acetoin + NADH
-
-
more than 99% enantiomeric excess of S-product
-
?
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH
-
-
more than 99% enantiomeric excess of S-product
-
?
methylglyoxal + NADH

lactaldehyde + NAD+
-
relative rate of reduction is 56% compared to reduction of dihydroxyacetone
-
-
?
methylglyoxal + NADH
lactaldehyde + NAD+
-
-
-
?
racemic 2,3-butanediol + NAD+

3-hydroxybutane-2-one + NADH + H+
-
-
-
?
racemic 2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH + H+
-
-
-
?
additional information

?
-
-
ability of the enzyme to use glycerol from biodiesel waste as substrate, overview
-
-
?
additional information
?
-
-
efficiency of a cofactor regeneration enzyme co-expressed with a glycerol dehydrogenase for the production of 1,3-dihydroxyacetone. In vitro biotransformation of glycerol is achieved with the cell-free extracts containing recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, or NADH oxidase LpNox1 from Lactobacillus pentosus, giving1,3-dihydroxyacetone, overview
-
-
?
additional information
?
-
enzyme is highly enantioselective towards S-isomers of substituted glycerol derivatives
-
-
-
additional information
?
-
-
enzyme is highly enantioselective towards S-isomers of substituted glycerol derivatives
-
-
-
additional information
?
-
the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview
-
-
?
additional information
?
-
the enzyme is also active with substrates 4-chloroacetoacetate, 3-chloroacetylpyridine, 4-chloroacetophenone, and acetophenone, substrate specificities of enzyme with bound Zn2+, Mn2+, or Mg2+, overview
-
-
?
additional information
?
-
-
high specificity of enzyme for secondary alcohols in R-configuration
-
-
?
additional information
?
-
-
no substrate: 1,3-propanediol, ethanol, 1-propanol, 2-propanol, propionic acid, 1,4-butanediol, sorbitol, L-iditol. Stereospecificity for R-form
-
-
?
additional information
?
-
-
high specificity of enzyme for secondary alcohols in R-configuration
-
-
?
additional information
?
-
-
no substrate: 1,3-propanediol, ethanol, 1-propanol, 2-propanol, propionic acid, 1,4-butanediol, sorbitol, L-iditol. Stereospecificity for R-form
-
-
?
additional information
?
-
-
enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60ưC in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60ưC, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0
-
-
?
additional information
?
-
-
enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60ưC in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60ưC, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0
-
-
?
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Ca2+
-
1 mM, stimulates 64.5% compared to 1 mM Mn2+
Co2+
-
presence of Mn2+ enhances the enzyme activity by 31.4%
Cu2+
-
presence of Mn2+ enhances the enzyme activity by 37.0%
Fe2+
-
1 mM, stimulates 26.3% compared to 1 mM Mn2+
Mg2+
improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview. The activity of Mn-GDH and Mg-GDH improves several folds in comparison to the native GDH. The activity of substituted GDH towards non-natural substrates, 4-chloroacetoacetate, 3-chloroacetylpyridine, p-chloroacetophenone, and acetophenone is 30folds higher than native GDH. Manganese substitution increases the half-life of GDH by 6folds at 60ưC and 70ưC
Na+
-
oxidation and reduction slightly increased
K+

-
required for enzymatic activity and glycerol binding
K+
-
oxidation of glycerol os greatly increased
K+
-
activates, less effective than NH4+
Li+

-
oxidation slightly increased
Mn2+

-
1 mM, activates
Mn2+
activates, polyethyleneimines-immobilized enzyme PEI-Mn2+-GDH exhibits a 2.9fold increase in activity compared with free GDH
Mn2+
improvement of activity by the substitution of a zinc ion with a manganese ion, accelerating the release of dioxyacetone
Mn2+
the enzyme demonstrates an improvement in activity by the substitution of a zinc ion with a manganese ion. Mn-GDH obeys a compulsory ordered-Bi-Bi mechanism
Mn2+
improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions Mn2+ and Mg2+, overview
Mn2+
-
increases activity significantly
Mn2+
-
presence of Mn2+ enhances the enzyme activity by 79.5%
NH4+

-
80% activation at 10 mM
NH4+
-
activates, 4fold increase in Vmax produced by NH4Cl in the direction of glycerol oxidation, and 70fold reduction in the Km for dihydroxyaceton and 2fold increase in the Vmax with 30 mM NH4Cl added to the dihydroxyaceton reduction reaction
Rb+

-
oxidation greatly increased
Zn2+

-
-
Zn2+
the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions
Zn2+
computer modeling suggests that the glycerol molecule is sandwiched by the Zn2+ and NAD+ ions
Zn2+
-
enzyme is dependent on Zn2+
Zn2+
a zinc-dependent metalloenzyme, improvement of activity by the substitution of a zinc ion with a manganese ion
Zn2+
glycerol dehydrogenase from Klebsiella pneumoniae sp. is a zinc-dependent metalloenzyme. The enzyme demonstrates an improvement in activity by the substitution of a zinc ion with a manganese ion
Zn2+
glycerol dehydrogenase from Klebsiella pneumoniae is a zinc-dependent metalloenzyme
Zn2+
-
1.6 mol Zn2+ bound per subunit
Zn2+
-
increases activity
Zn2+
-
active-site zinc responsible for coordinating glycerol in the active site of the enzyme. The active site is highly conserved and contains a zinc ion coordinated by two histidines and an aspartate
Zn2+
-
one ion per monomer, crystallization data
Zn2+
1.9fold increase in activity in presence of Zn2+
additional information

-
comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH
additional information
comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH
additional information
-
the equilibrium constants for each ligand-binding are calculated by using the forward and reverse rate constants. By profiling the binding rate and energy for substrate and product with enzyme, the rate accelerating step is determined
additional information
the equilibrium constants for each ligand-binding are calculated by using the forward and reverse rate constants. By profiling the binding rate and energy for substrate and product with enzyme, the rate accelerating step is determined
additional information
the natural GDH-bound Zn2+ are substituted with several divalent metal ions and the enzyme activity is significantly altered. Cu2+, Ni2+, Zn2+, Mn2+, Mg2+ and Ca2+ are used to investigate the effects of metal ions on GDH activity. Only Mn2+ improves the GDH activity by 1.1fold, whereas the other five metal ions inhibit the enzyme to varying degrees at high concentrations
additional information
bifunctional role of metal ions in GDH in catalysis and structure stabilization
additional information
-
three highly conserved enzyme residues, Asp171, His254, and His271, are associated with metal ion binding
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1,3-Propanediol
-
competitive inhibitor versus glycerol in direction of glycerol oxidation, noncompetitive inhibitor versus NAD+, competitive inhibitor versus dihydroxyacetone in direction of glycerol reduction, noncompetitive inhibitor versus NADH
1-ethyl-3(3-dimethylaminopropyl)carbodiimide
-
-
2,2'dipyridyl
-
1 mM, complete inhibition
2,4,6-Trinitrobenzene sulfonate
-
-
2-amino-2-(hydroxymethyl)-1,3-propanediol
-
strong inhibition, IC50 2 mM
acetone
-
inactivation, enzyme regains activity after removal of ketone
ADP
-
3 mM, 10% inhibition
AMP
-
3 mM, 13% inhibition
ATP
-
3 mM, 6% inhibition
catechol
-
i.e. 1,2-butanediol, inactivation, enzyme regains activity after removal of alcohol
Cd2+
-
strongly inhibitory
Cetylpyridinium chloride
-
strong inhibition at low concentration
cetyltrimethylammonium bromide
-
strong inhibition at low concentration
diacetyl
-
inactivation, enzyme regains activity after removal of ketone
diethyldithiocarbamate
-
slight inhibition, 2 mM, 10 mM
dihydroxyacetone phosphate
-
-
dimethylformamide
-
inactivation
Dimethylsulfoxide
-
inactivation
dioxane
-
inactivation, enzyme regains activity after removal of ketone
ethanol
-
10% v/v: 25-75% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
ethylene glycol
-
strong inhibition, IC50 4 mM
iodoacetamide
-
strong inhibition, 10 mM
isobutanol
-
5% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
K+
-
reduction of dihydroxyacetone
Li+
-
competitive, forward reaction
methanol
-
10% v/v: 25-75% loss of activity, 5% v/v, 50-95% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
methylene blue
-
enzyme activity is decreased by photooxidation
Mg2+
inhibits the enzyme at high concentrations
n-amyl alcohol
-
2% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
n-butanol
-
5% v/v: 0-50% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
n-Propanol
-
5% v/v: 25-60% loss of activity, depending on substrate, enzyme regains activity after removal of alcohol
Na+
-
competitive, forward reaction
Ni2+
inhibits the enzyme at high concentrations
o-phthalaldehyde
-
inactivation due to intramolecular thioisoindole formation, glycerol partially protects
p-hydroxymercuribenzoate
-
0.1 mM, strong
Phenanthroline
-
1 mM, complete inhibition
polyethyleneimines
activating at 0.5 mM, inhibitory at 1 mM
-
pyridin-2,6-dicarboxylic acid
-
-
pyridoxyl-5'-phosphate
-
inactivation, NAD+ or NADH protect
Sodium dodecyl sulfate
-
-
sodium tetraborate
-
1 mM, 53% inhibition
Tris HCl
Tris buffer lowers the enzyme activity about 7fold in comparison to CHES buffer
Tris(hydroxymethyl)aminomethane
competitive with respect to glycerol
1,10-phenanthroline

-
1 mM
2,2'-bipyridyl

-
powerful inhibition
2-mercaptoethanol

-
strongly inhibitory at 100 mM, but slight activation in lower concentration, 1 mM
2-mercaptoethanol
-
strong inhibition, IC50 0.3 mM
8-Quinolinol

-
1 mM, 10 mM
Ca2+

inhibits the enzyme at high concentrations
Cu2+

-
strong inhibition
Cu2+
inhibits the enzyme at high concentrations
dihydroxyacetone

-
noncompatible inhibitor, at saturated level of glycerol
dihydroxyacetone
-
above 0.5 mM
dihydroxyacetone
noncompetitive product inhibition; noncompetitive product inhibition with respect to NAD+
dithiothreitol

-
slight inhibition
EDTA

-
3 mM, 30 mM
EDTA
-
slight inhibition, 10 mM
EDTA
nearly complete inhibition
Fe3+

-
-
L-cysteine

-
slight inhibition
N-ethylmaleimide

-
-
N-ethylmaleimide
-
rapid inactivation, IC50: 0.2 mM
NADH

-
-
NADH
-
competitive inhibitor versus NAD+ in direction of glycerol oxidation, noncompetitive inhibitor versus glycerol
NADH
competitive product inhibition; competitive product inhibition
NADH
-
product inhibition , competitive with NAD+
NADP+

-
-
NADP+
-
inhibits oxidation of glycerol
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
95% inhibition at 0.01 mM
Zn2+

-
strong inhibitory
Zn2+
-
over 90% inhibition at 0.01 mM
Zn2+
-
50% inhibition at 0.021 mM
Zn2+
inhibits the enzyme at high concentrations
Zn2+
-
inhibits 24% at 1 mM
additional information

-
enzyme inhibition simulations, overview
-
additional information
enzyme inhibition simulations, overview
-
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Acidosis
Hormonal regulation of glutamine metabolism by OK cells.
Adrenocortical Hyperfunction
Effect of serum storage, anti-inflammatory oral doses of prednisone, and spontaneous hyperadrenocorticism on serum glutamate dehydrogenase activity in dogs.
Brain Neoplasms
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
Carcinogenesis
Glutaminolysis and carcinogenesis of oral squamous cell carcinoma.
Carcinoma
Changes in serum enzyme activity after transcatheter arterial embolization for hepatic neoplasm.
Carcinoma, Hepatocellular
Changes in serum enzyme activity after transcatheter arterial embolization for hepatic neoplasm.
Carcinoma, Hepatocellular
Multiplexing cell viability assays.
Chemical and Drug Induced Liver Injury
A longitudinal assessment of miR-122 and GLDH as biomarkers of drug-induced liver injury in the rat.
Chemical and Drug Induced Liver Injury
Biomarkers of mitotoxicity after acute liver injury: Further insights into the interpretation of glutamate dehydrogenase.
Chemical and Drug Induced Liver Injury
Glutamate dehydrogenase as a biomarker for mitotoxicity; insights from furosemide hepatotoxicity in the mouse.
Chemical and Drug Induced Liver Injury
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Cholestasis
Activities of APh, gamma-GT, GlDH and GPT and bile acid concentrations in serum after bile duct obstruction and cycloheximide in the rat.
Cholestasis
The serum activities of AP, gamma-GT, GlDH and GPT after bile duct obstruction and ethionine in the rat.
Dystocia
Effects of dystocia, fetotomy and caesarian sections on the liver enzymes activities and concentrations of some serum biochemical parameters in dairy cattle.
Eosinophilia
Host responses during experimental infection with Fasciola gigantica and Fasciola hepatica in Merino sheep II. Development of a predictive index for Fasciola gigantica worm burden.
Eosinophilia
Pre-exposure of cattle to drug-abbreviated Fasciola hepatica infections: the effect upon subsequent challenge infection and the early immune response.
Exanthema
D-penicillamine-induced granulomatous hepatitis in brown Norway rats.
Fatty Liver
[Increased gamma-GT, minimal changes in liver histology, abdominal complaints--a functional liver liver disease]
Hemoglobinuria
Serum glutamic oxalacetic transaminase, glutamic pyruvic transaminase, gamma-glutamyl transpeptidase and glutamic dehydrogenase levels in favism.
Hepatic Encephalopathy
A study of lipid peroxidation and vitamin E in dairy cows with hepatic insufficiency.
Hepatitis
D-penicillamine-induced granulomatous hepatitis in brown Norway rats.
Hepatitis
[Diagnostic and prognostic significance of massively increased serum glutamate dehydrogenase activity]
Hepatitis, Autoimmune
Relation between autoimmune liver diseases and viral hepatitis: clinical and serological characteristics in 859 patients.
Infections
Acquisition of resistance against Fasciola gigantica by Indonesian thin tail sheep.
Infections
An experimental study on triclabendazole resistance of Fasciola hepatica in sheep.
Infections
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Infections
Response of sheep to challenge infection with Fasciola hepatica.
Ketosis
Common and specific mineral and metabolic features in dairy cows with clinical metritis, hypocalcaemia or ketosis.
Leukopenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Liver Failure
A study of lipid peroxidation and vitamin E in dairy cows with hepatic insufficiency.
Lymphopenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Meningitis
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
Meningitis
Tentative identification of glycerol dehydrogenase as Escherichia coli K1 virulence factor cglD and its involvement in the pathogenesis of experimental neonatal meningitis.
Muscular Dystrophies
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Muscular Dystrophy, Duchenne
Safety and disease monitoring biomarkers in Duchenne muscular dystrophy: results from a Phase II trial.
Neoplasm Metastasis
Alpha 1 isoenzyme of alkaline phosphatases. Clinical importance and value for the detection of liver metastases.
Neutropenia
Epidemiology, genetic variants and clinical course of natural infections with Anaplasma phagocytophilum in a dairy cattle herd.
Pancreatitis
[Impairment of glycerophosphate and glycerol turnover in myocardium under conditions of experimental pancreatitis]
Pneumonia
A non-pathogenic and optically high concentrated (R,R)-2,3-butanediol biosynthesizing Klebsiella strain.
Rhabdomyolysis
Serum glutamate dehydrogenase activity enables early detection of liver injury in subjects with underlying muscle impairments.
Scabies
Histology of the skin and determination of blood and serum parameters during the recovery phase of sarcoptic manage in cattle after avermectin (Ivomec) treatment.
Toxemia
[Value of placental enzymes, endocrinologic parameters of pregnancy and placental perfusion in cases of intrauterine growth retardation]
Tuberculosis, Meningeal
Levels of glutamic acid decarboxylase (GAD), gamma amino butyric acid transaminase (GABA-T), glutamic acid dehydrogenase (GLDH) and proteins in cerebrospinal fluid of certain neurological disorders.
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0.06 - 0.202
1,2-propanediol
11.9 - 77.8
1,3-butanediol
71
1,4-Butanediol
-
pH and temperature not specified in the publication
840
1-butanol
-
pH and temperature not specified in the publication
840
1-Octanol
-
pH and temperature not specified in the publication
3
1-phenylethanol
-
pH and temperature not specified in the publication
46
1-propanol
-
pH and temperature not specified in the publication
0.0238
2,3-Butanediol
-
-
0.3
2-butanol
-
pH and temperature not specified in the publication
4
2-propanol
-
pH and temperature not specified in the publication
78 - 281
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
-
180
3-amino-1,2-propanediol
-
pH 8.8, 25ưC
6.1
3-bromo-1,2-propanediol
-
pH 8.8, 25ưC
162
3-butoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
6
3-Chloro-1,2-propanediol
-
pH 8.8, 25ưC
13.4 - 371
3-ethoxypropane-1,2-diol
-
4
3-mercapto-1,2-propanediol
-
pH 8.8, 25ưC
45 - 977
3-methoxypropane-1,2-diol
-
7
3-phenoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
30 - 608
3-propoxypropane-1,2-diol
-
31.2 - 707
3-[(propan-2-yl)oxy]propane-1,2-diol
-
76
benzyl alcohol
-
pH and temperature not specified in the publication
67.3
butane-2,3-diol
pH 7.4, 35ưC
1 - 19
D-1,2-propanediol
-
6.5 - 90
D-2,3-butanediol
0.07
D-glyceraldehyde
-
pH and temperature not specified in the publication
0.06 - 4.87
dihydroxyacetone
35
ethanol
-
pH and temperature not specified in the publication
56 - 92.7
ethylene glycol
0.08 - 2.9
N6-carboxymethyl-NAD+
4.4
R-1-amino-2-propanol
-
pH 8.8, 25ưC
67.3
racemic 2,3-butanediol
at pH 8.6 and 35ưC
-
500
S-1-amino-2-propanol
-
pH 8.8, 25ưC
additional information
additional information
-
3
1,2-Butanediol

wild-type, pH 8.9, 55ưC
4
1,2-Butanediol
mutant D121N, pH 8.9, 55ưC
44
1,2-Butanediol
mutant /D121NF245S, pH 8.9, 55ưC
23.5
1,2-Butanediol
mutant F245S, pH 8.9, 55ưC
0.06
1,2-propanediol

-
pH 8.8, 25ưC
0.202
1,2-propanediol
-
-
20.9
1,3-butanediol

-
pH 9.5, 30ưC
11.9
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30ưC
16.2
1,3-butanediol
-
wild type protein, pH 9.5, 30ưC
29.2
1,3-butanediol
-
pH 9.5, 30ưC
49.9
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30ưC
77.8
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30ưC
78
3-(2,2,2-trifluoroethoxy)propane-1,2-diol

wild-type, pH 7.0, 30ưC
-
281
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
13.4
3-ethoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
371
3-ethoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
45
3-methoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
977
3-methoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
30
3-propoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
608
3-propoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
31.2
3-[(propan-2-yl)oxy]propane-1,2-diol

wild-type, pH 7.0, 30ưC
-
707
3-[(propan-2-yl)oxy]propane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
1
D-1,2-propanediol

wild-type, pH 8.9, 55ưC
-
8
D-1,2-propanediol
mutant /D121NF245S, pH 8.9, 55ưC
-
4.5
D-1,2-propanediol
mutant F245S, pH 8.9, 55ưC
-
19
D-1,2-propanediol
mutant D121N, pH 8.9, 55ưC
-
17
D-2,3-butanediol

wild-type, pH 8.9, 55ưC
6.5
D-2,3-butanediol
mutant F245S, pH 8.9, 55ưC
90
D-2,3-butanediol
mutant D121N, pH 8.9, 55ưC
39
D-2,3-butanediol
mutant /D121NF245S, pH 8.9, 55ưC
0.06
dihydroxyacetone

-
pH 6.0
2
dihydroxyacetone
-
pH 9.1, 37ưC, mutant D
2
dihydroxyacetone
-
mutant enzyme E5-MD, at pH 9.1 and 37ưC
0.77
dihydroxyacetone
-
25ưC
1.18
dihydroxyacetone
-
pH 9.1, 37ưC, wild-type enzyme
1.18
dihydroxyacetone
-
wild type enzyme, at pH 9.1 and 37ưC
0.385
dihydroxyacetone
-
-
0.385
dihydroxyacetone
-
pH 6.0, 25ưC
4.87
dihydroxyacetone
-
-
56
ethylene glycol

-
pH and temperature not specified in the publication
92.7
ethylene glycol
pH 7.4, 35ưC
92.7
ethylene glycol
at pH 8.6 and 35ưC
0.5
glycerol

-
pH 10.0
0.2
glycerol
-
pH and temperature not specified in the publication
0.8
glycerol
-
pH 10, 35ưC
1.4
glycerol
-
pH 9.0, 25ưC
4
glycerol
wild-type, pH 8.9, 55ưC
26
glycerol
pH 10.0, 30ưC, immobilized enzyme
50
glycerol
wild-type, pH 7.0, 30ưC
5.1
glycerol
-
pH 8.8, 25ưC
19.4
glycerol
recombinant chimeric enzyme GDH-NOX, pH 11.0, 37ưC
41
glycerol
mutant F245S, pH 8.9, 55ưC
91
glycerol
pH 7.4, 35ưC
91
glycerol
at pH 8.6 and 35ưC
10.9
glycerol
-
pH 9.0, 25ưC
148
glycerol
mutant /D121NF245S, pH 8.9, 55ưC
47
glycerol
-
pH 10.3, 30ưC, recombinant enzyme, in presence of 20 mM KCl
76
glycerol
-
pH 10.3, 30ưC, recombinant enzyme
21.6
glycerol
pH 10.0, 30ưC, free enzyme
81
glycerol
-
pH 10.3, 30ưC, recombinant enzyme, in presence of 30 mM NH4Cl
73.3
glycerol
-
pH 9.7, 37ưC, mutant D 76.3 mM
74.3
glycerol
-
in the presence of NH4+
91.7
glycerol
-
pH 9.7, 37ưC, wild-type enzyme
48.9
glycerol
pH 7.5, 25ưC
195
glycerol
mutant D121N, pH 8.9, 55ưC
30.29
glycerol
-
pH 8.0, 60ưC, recombinant enzyme
1880
glycerol
mutant L252A, pH 7.0, 30ưC
0.22
Glycerone

-
pH 6.5, 30ưC, recombinant enzyme, in presence of 30 mM NH4Cl
0.15
Glycerone
-
pH 6.5, 30ưC, recombinant enzyme
0.24
Glycerone
-
pH 6.5, 30ưC, recombinant enzyme, in presence of 20 mM KCl
1.08
Glycerone
-
pH 6.0, 60ưC, recombinant enzyme
0.25
N6-carboxymethyl-NAD+

pH 7.4, 50ưC, recombinant mutant V44A/K157G
0.25
N6-carboxymethyl-NAD+
mutant enzyme V44A/K157G, at pH 7.4 and 50ưC
0.37
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant wild-type enzyme
0.37
N6-carboxymethyl-NAD+
wild type enzyme, at pH 7.4 and 50ưC
0.15
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant V44A
0.15
N6-carboxymethyl-NAD+
mutant enzyme V44A, at pH 7.4 and 50ưC
1.5
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant I154A/K157G
1.5
N6-carboxymethyl-NAD+
mutant enzyme I154A/K157G, at pH 7.4 and 50ưC
0.08
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant K157G
0.08
N6-carboxymethyl-NAD+
mutant enzyme K157G, at pH 7.4 and 50ưC
0.36
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant K157N
0.36
N6-carboxymethyl-NAD+
mutant enzyme K157N, at pH 7.4 and 50ưC
2.3
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant V44A/I154A/K157G
2.3
N6-carboxymethyl-NAD+
mutant enzyme V44A/I154A/K157G, at pH 7.4 and 50ưC
0.73
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant I154A
0.73
N6-carboxymethyl-NAD+
mutant enzyme I154A, at pH 7.4 and 50ưC
2.9
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant V44A/I154A
2.9
N6-carboxymethyl-NAD+
mutant enzyme V44A/ I154A, at pH 7.4 and 50ưC
0.186
N6-carboxymethyl-NAD+
pH 7.4, 50ưC, recombinant mutant V44A/K157N
0.186
N6-carboxymethyl-NAD+
mutant enzyme V44A/ K157N, at pH 7.4 and 50ưC
0.089
NAD+

-
pH 9.0, 25ưC
0.3
NAD+
-
pH 9.0, 25ưC
0.6
NAD+
pH 7.4, 50ưC, recombinant mutant V44A/I154A/K157G
0.015
NAD+
-
pH and temperature not specified in the publication
0.021
NAD+
pH 7.4, 50ưC, recombinant mutant V44A/K157G
0.025
NAD+
pH 7.4, 50ưC, recombinant mutant K157N
0.07
NAD+
pH 7.4, 50ưC, recombinant mutant V44A
0.4
NAD+
wild-type, pH 8.9, 55ưC
1
NAD+
-
pH 10.3, 30ưC, recombinant enzyme, in presence of 30 mM NH4Cl
0.22
NAD+
pH 7.5, 25ưC
0.23
NAD+
Mg-GDH, pH 12.0, 45ưC, recombinant enzyme
1.5
NAD+
mutant D121N, pH 8.9, 55ưC
0.7
NAD+
mutant F245S, pH 8.9, 55ưC
0.81
NAD+
-
pH 10.3, 30ưC, recombinant enzyme
0.024
NAD+
pH 7.4, 50ưC, recombinant wild-type enzyme
2.3
NAD+
mutant /D121NF245S, pH 8.9, 55ưC
4.7
NAD+
-
pH 9.7, 37ưC, mutant D
0.031
NAD+
pH 7.4, 50ưC, recombinant mutant K157G
0.38
NAD+
wild-type Zn-GDH, pH 12.0, 45ưC, recombinant enzyme
0.108
NAD+
pH 7.4, 50ưC, recombinant mutant I154A/K157G
2.6
NAD+
at pH 8.6 and 35ưC
0.039
NAD+
pH 7.4, 50ưC, recombinant mutant V44A/K157N
0.051
NAD+
pH 7.9, 50ưC, recombinant wild-type enzyme
1.12
NAD+
Mg-GDH, pH 12.0, 45ưC, recombinant enzyme
3.2
NAD+
-
pH 10.3, 30ưC, recombinant enzyme, in presence of 20 mM KCl
0.351
NAD+
pH 7.4, 50ưC, recombinant mutant V44A/I154A
0.0182
NAD+
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30ưC
0.088
NAD+
pH 7.4, 50ưC, recombinant mutant I154A
0.0165
NAD+
-
wild type protein, pH 9.5, 30ưC
4.07
NAD+
-
pH 9.7, 37ưC, wild-type enzyme
0.5946
NAD+
-
mutant protein D121A, pH 9.5, 30ưC
0.4614
NAD+
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30ưC
0.05
NADH

-
pH 6.5, 30ưC, recombinant enzyme
0.05
NADH
wild-type, pH 5.4, 55ưC
0.06
NADH
-
pH 6.0, 60ưC, recombinant enzyme
0.1
NADH
mutant D121N, pH 5.4, 55ưC
0.1
NADH
mutant F245S, pH 5.4, 55ưC
0.3
NADH
mutant /D121NF245S, pH 5.9, 55ưC
0.005
NADH
-
pH and temperature not specified in the publication
0.02
NADH
pH 7.9, 50ưC, recombinant wild-type enzyme
0.07
NADH
-
pH 6.5, 30ưC, recombinant enzyme, in presence of 20 mM KCl
0.12
NADH
-
pH 9.1, 37ưC, mutant D
0.08
NADH
-
pH 9.1, 37ưC, wild-type enzyme
0.08
NADH
-
pH 6.5, 30ưC, recombinant enzyme, in presence of 30 mM NH4Cl
0.0513
NADH
recombinant chimeric enzyme GDH-NOX, pH 11.0, 37ưC
55.5
pyruvate

mutant /D121NF245S, pH 5.9, 55ưC
54.5
pyruvate
mutant F245S, pH 5.4, 55ưC
207
pyruvate
wild-type, pH 5.4, 55ưC
60.5
pyruvate
mutant D121N, pH 5.4, 55ưC
additional information
additional information

-
kinetic study with different effectors, overview
-
additional information
additional information
kinetic and thermodynamic analysis, Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview
-
additional information
additional information
kinetic model based on an ordered bi-bi mechanism, thermodynamics, simulations, overview
-
additional information
additional information
-
kinetic modeling based on an ordered Bi-Bi mechanism, nonlinear regression-based kinetic parameter estimation. Thermodynamics, overview
-
additional information
additional information
kinetic modeling based on an ordered Bi-Bi mechanism, nonlinear regression-based kinetic parameter estimation. Thermodynamics, overview
-
additional information
additional information
kinetic study of the metal ion-chelated polyethyleneimines-immobilized enzyme
-
additional information
additional information
Michaelis-Menten kinetics, cooperative behavior of TmGlyDH
-
additional information
additional information
-
Michaelis-Menten kinetics, cooperative behavior of TmGlyDH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
50 - 120.5
1,2-Butanediol
2.6 - 87.2
1,3-butanediol
0.32 - 14
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
-
1.3
3-butoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
0.19 - 31
3-ethoxypropane-1,2-diol
-
0.84 - 6.6
3-methoxypropane-1,2-diol
-
0.7
3-phenoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.27 - 12
3-propoxypropane-1,2-diol
-
0.3 - 13
3-[(propan-2-yl)oxy]propane-1,2-diol
-
22.5
butane-2,3-diol
pH 7.4, 35ưC
29 - 92
D-1,2-propanediol
-
10.5 - 136
D-2,3-butanediol
98.44
Glycerone
-
pH 6.0, 60ưC, recombinant enzyme
22.5
racemic 2,3-butanediol
at pH 8.6 and 35ưC
-
50
1,2-Butanediol

mutant /D121NF245S, pH 8.9, 55ưC
71
1,2-Butanediol
mutant F245S, pH 8.9, 55ưC
66.5
1,2-Butanediol
mutant D121N, pH 8.9, 55ưC
120.5
1,2-Butanediol
wild-type, pH 8.9, 55ưC
3.3
1,3-butanediol

-
wild type protein, pH 9.5, 30ưC
2.6
1,3-butanediol
-
pH 9.5, 30ưC
2.7
1,3-butanediol
-
pH 9.5, 30ưC
9.1
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30ưC
87.2
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30ưC
62.4
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30ưC
14
3-(2,2,2-trifluoroethoxy)propane-1,2-diol

mutant L252A, pH 7.0, 30ưC
-
0.32
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.19
3-ethoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
31
3-ethoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
0.84
3-methoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
6.6
3-methoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
12
3-propoxypropane-1,2-diol

mutant L252A, pH 7.0, 30ưC
-
0.27
3-propoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.3
3-[(propan-2-yl)oxy]propane-1,2-diol

wild-type, pH 7.0, 30ưC
-
13
3-[(propan-2-yl)oxy]propane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
42.5
D-1,2-propanediol

mutant /D121NF245S, pH 8.9, 55ưC
-
92
D-1,2-propanediol
wild-type, pH 8.9, 55ưC
-
29
D-1,2-propanediol
mutant D121N, pH 8.9, 55ưC
-
87.5
D-1,2-propanediol
mutant F245S, pH 8.9, 55ưC
-
10.5
D-2,3-butanediol

mutant D121N, pH 8.9, 55ưC
57.5
D-2,3-butanediol
mutant /D121NF245S, pH 8.9, 55ưC
136
D-2,3-butanediol
mutant F245S, pH 8.9, 55ưC
50.5
D-2,3-butanediol
wild-type, pH 8.9, 55ưC
2.8
ethylene glycol

pH 7.4, 35ưC
2.8
ethylene glycol
at pH 8.6 and 35ưC
9
glycerol

mutant L252A, pH 7.0, 30ưC
7.4
glycerol
wild-type, pH 7.0, 30ưC
50
glycerol
mutant D121N, pH 8.9, 55ưC
1.89
glycerol
-
pH 8.0, 60ưC, recombinant enzyme
42.5
glycerol
mutant F245S, pH 8.9, 55ưC
11
glycerol
mutant /D121NF245S, pH 8.9, 55ưC
3.36
glycerol
pH 10.0, 30ưC, immobilized enzyme
2.06
glycerol
pH 10.0, 30ưC, free enzyme
117.5
glycerol
wild-type, pH 8.9, 55ưC
87.1
glycerol
pH 7.4, 35ưC
87.1
glycerol
at pH 8.6 and 35ưC
70.6
NAD+

pH 7.4, 35ưC
70.6
NAD+
at pH 8.6 and 35ưC
1.5
pyruvate

mutant D121N, pH 5.4, 55ưC
10.5
pyruvate
wild-type, pH 5.4, 55ưC
352
pyruvate
mutant F245S, pH 5.4, 55ưC
165
pyruvate
mutant /D121NF245S, pH 5.9, 55ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.09 - 1.26
1,3-butanediol
0.004 - 0.051
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
-
0.008
3-butoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
0.014 - 0.085
3-ethoxypropane-1,2-diol
-
0.007 - 0.019
3-methoxypropane-1,2-diol
-
0.112
3-phenoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.009 - 0.019
3-propoxypropane-1,2-diol
-
0.01 - 0.018
3-[(propan-2-yl)oxy]propane-1,2-diol
-
0.33
butane-2,3-diol
pH 7.4, 35ưC
1.5 - 92
D-1,2-propanediol
-
0.1 - 21
D-2,3-butanediol
91.15
Glycerone
-
pH 6.0, 60ưC, recombinant enzyme
0.33
racemic 2,3-butanediol
at pH 8.6 and 35ưC
-
1
1,2-Butanediol

mutant /D121NF245S, pH 8.9, 55ưC
3
1,2-Butanediol
mutant F245S, pH 8.9, 55ưC
40
1,2-Butanediol
wild-type, pH 8.9, 55ưC
15.5
1,2-Butanediol
mutant D121N, pH 8.9, 55ưC
0.2
1,3-butanediol

-
wild type protein, pH 9.5, 30ưC
0.09
1,3-butanediol
-
pH 9.5, 30ưC
1.12
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30ưC
0.12
1,3-butanediol
-
pH 9.5, 30ưC
0.77
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30ưC
1.26
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30ưC
0.004
3-(2,2,2-trifluoroethoxy)propane-1,2-diol

wild-type, pH 7.0, 30ưC
-
0.051
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
0.085
3-ethoxypropane-1,2-diol

mutant L252A, pH 7.0, 30ưC
-
0.014
3-ethoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.019
3-methoxypropane-1,2-diol

wild-type, pH 7.0, 30ưC
-
0.007
3-methoxypropane-1,2-diol
mutant L252A, pH 7.0, 30ưC
-
0.019
3-propoxypropane-1,2-diol

mutant L252A, pH 7.0, 30ưC
-
0.009
3-propoxypropane-1,2-diol
wild-type, pH 7.0, 30ưC
-
0.018
3-[(propan-2-yl)oxy]propane-1,2-diol

mutant L252A, pH 7.0, 30ưC
-
0.01
3-[(propan-2-yl)oxy]propane-1,2-diol
wild-type, pH 7.0, 30ưC
-
20
D-1,2-propanediol

mutant F245S, pH 8.9, 55ưC
-
5.5
D-1,2-propanediol
mutant /D121NF245S, pH 8.9, 55ưC
-
1.5
D-1,2-propanediol
mutant D121N, pH 8.9, 55ưC
-
92
D-1,2-propanediol
wild-type, pH 8.9, 55ưC
-
1.5
D-2,3-butanediol

mutant /D121NF245S, pH 8.9, 55ưC
21
D-2,3-butanediol
mutant F245S, pH 8.9, 55ưC
0.1
D-2,3-butanediol
mutant D121N, pH 8.9, 55ưC
3
D-2,3-butanediol
wild-type, pH 8.9, 55ưC
0.03
ethylene glycol

at pH 8.6 and 35ưC
0.03
ethylene glycol
pH 7.4, 35ưC
129
glycerol

pH 10.0, 30ưC, immobilized enzyme
0.06
glycerol
-
pH 8.0, 60ưC, recombinant enzyme
30
glycerol
wild-type, pH 8.9, 55ưC
0.3
glycerol
mutant D121N, pH 8.9, 55ưC
94
glycerol
pH 10.0, 30ưC, free enzyme
1
glycerol
mutant F245S, pH 8.9, 55ưC
0.005
glycerol
mutant L252A, pH 7.0, 30ưC
0.1
glycerol
mutant /D121NF245S, pH 8.9, 55ưC
0.96
glycerol
at pH 8.6 and 35ưC
0.96
glycerol
pH 7.4, 35ưC
0.148
glycerol
wild-type, pH 7.0, 30ưC
200
NAD+

-
wild type protein, pH 9.5, 30ưC
188
NAD+
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30ưC
120.3
NAD+
Mg-GDH, pH 12.0, 45ưC, recombinant enzyme
105
NAD+
-
mutant protein D121A, pH 9.5, 30ưC
500
NAD+
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30ưC
27
NAD+
at pH 8.6 and 35ưC
46.1
NAD+
wild-type Zn-GDH, pH 12.0, 45ưC, recombinant enzyme
83.6
NAD+
Mg-GDH, pH 12.0, 45ưC, recombinant enzyme
0.05
pyruvate

wild-type, pH 5.4, 55ưC
6.5
pyruvate
mutant F245S, pH 5.4, 55ưC
0.02
pyruvate
mutant D121N, pH 5.4, 55ưC
3
pyruvate
mutant /D121NF245S, pH 5.9, 55ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.