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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 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, 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 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, 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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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, 25°C
6.1
3-bromo-1,2-propanediol
-
pH 8.8, 25°C
162
3-butoxypropane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
6
3-Chloro-1,2-propanediol
-
pH 8.8, 25°C
13.4 - 371
3-ethoxypropane-1,2-diol
-
4
3-mercapto-1,2-propanediol
-
pH 8.8, 25°C
45 - 977
3-methoxypropane-1,2-diol
-
7
3-phenoxypropane-1,2-diol
wild-type, pH 7.0, 30°C
-
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, 35°C
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, 25°C
67.3
racemic 2,3-butanediol
at pH 8.6 and 35°C
-
500
S-1-amino-2-propanol
-
pH 8.8, 25°C
additional information
additional information
-
3
1,2-Butanediol
wild-type, pH 8.9, 55°C
4
1,2-Butanediol
mutant D121N, pH 8.9, 55°C
23.5
1,2-Butanediol
mutant F245S, pH 8.9, 55°C
44
1,2-Butanediol
mutant /D121NF245S, pH 8.9, 55°C
0.06
1,2-propanediol
-
pH 8.8, 25°C
0.202
1,2-propanediol
-
-
11.9
1,3-butanediol
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30°C
16.2
1,3-butanediol
-
wild type protein, pH 9.5, 30°C
20.9
1,3-butanediol
-
pH 9.5, 30°C
29.2
1,3-butanediol
-
pH 9.5, 30°C
49.9
1,3-butanediol
-
mutant protein D121A, pH 9.5, 30°C
77.8
1,3-butanediol
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C
78
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
wild-type, pH 7.0, 30°C
-
281
3-(2,2,2-trifluoroethoxy)propane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
13.4
3-ethoxypropane-1,2-diol
wild-type, pH 7.0, 30°C
-
371
3-ethoxypropane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
45
3-methoxypropane-1,2-diol
wild-type, pH 7.0, 30°C
-
977
3-methoxypropane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
30
3-propoxypropane-1,2-diol
wild-type, pH 7.0, 30°C
-
608
3-propoxypropane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
31.2
3-[(propan-2-yl)oxy]propane-1,2-diol
wild-type, pH 7.0, 30°C
-
707
3-[(propan-2-yl)oxy]propane-1,2-diol
mutant L252A, pH 7.0, 30°C
-
1
D-1,2-propanediol
wild-type, pH 8.9, 55°C
-
4.5
D-1,2-propanediol
mutant F245S, pH 8.9, 55°C
-
8
D-1,2-propanediol
mutant /D121NF245S, pH 8.9, 55°C
-
19
D-1,2-propanediol
mutant D121N, pH 8.9, 55°C
-
6.5
D-2,3-butanediol
mutant F245S, pH 8.9, 55°C
17
D-2,3-butanediol
wild-type, pH 8.9, 55°C
39
D-2,3-butanediol
mutant /D121NF245S, pH 8.9, 55°C
90
D-2,3-butanediol
mutant D121N, pH 8.9, 55°C
0.06
dihydroxyacetone
-
pH 6.0
0.385
dihydroxyacetone
-
-
0.385
dihydroxyacetone
-
pH 6.0, 25°C
0.77
dihydroxyacetone
-
25°C
1.18
dihydroxyacetone
-
pH 9.1, 37°C, wild-type enzyme
1.18
dihydroxyacetone
-
wild type enzyme, at pH 9.1 and 37°C
2
dihydroxyacetone
-
pH 9.1, 37°C, mutant D
2
dihydroxyacetone
-
mutant enzyme E5-MD, at pH 9.1 and 37°C
4.87
dihydroxyacetone
-
-
56
ethylene glycol
-
pH and temperature not specified in the publication
92.7
ethylene glycol
pH 7.4, 35°C
92.7
ethylene glycol
at pH 8.6 and 35°C
0.2
glycerol
-
pH and temperature not specified in the publication
0.8
glycerol
-
pH 10, 35°C
1.4
glycerol
-
pH 9.0, 25°C
4
glycerol
wild-type, pH 8.9, 55°C
5.1
glycerol
-
pH 8.8, 25°C
10.9
glycerol
-
pH 9.0, 25°C
19.4
glycerol
recombinant chimeric enzyme GDH-NOX, pH 11.0, 37°C
21.6
glycerol
pH 10.0, 30°C, free enzyme
26
glycerol
pH 10.0, 30°C, immobilized enzyme
30.29
glycerol
-
pH 8.0, 60°C, recombinant enzyme
41
glycerol
mutant F245S, pH 8.9, 55°C
47
glycerol
-
pH 10.3, 30°C, recombinant enzyme, in presence of 20 mM KCl
48.9
glycerol
pH 7.5, 25°C
50
glycerol
wild-type, pH 7.0, 30°C
73.3
glycerol
-
pH 9.7, 37°C, mutant D 76.3 mM
74.3
glycerol
-
in the presence of NH4+
76
glycerol
-
pH 10.3, 30°C, recombinant enzyme
81
glycerol
-
pH 10.3, 30°C, recombinant enzyme, in presence of 30 mM NH4Cl
91
glycerol
at pH 8.6 and 35°C
91.7
glycerol
-
pH 9.7, 37°C, wild-type enzyme
148
glycerol
mutant /D121NF245S, pH 8.9, 55°C
195
glycerol
mutant D121N, pH 8.9, 55°C
1880
glycerol
mutant L252A, pH 7.0, 30°C
0.15
Glycerone
-
pH 6.5, 30°C, recombinant enzyme
0.22
Glycerone
-
pH 6.5, 30°C, recombinant enzyme, in presence of 30 mM NH4Cl
0.24
Glycerone
-
pH 6.5, 30°C, recombinant enzyme, in presence of 20 mM KCl
1.08
Glycerone
-
pH 6.0, 60°C, recombinant enzyme
0.08
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant K157G
0.08
N6-carboxymethyl-NAD+
mutant enzyme K157G, at pH 7.4 and 50°C
0.15
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A
0.15
N6-carboxymethyl-NAD+
mutant enzyme V44A, at pH 7.4 and 50°C
0.186
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157N
0.186
N6-carboxymethyl-NAD+
mutant enzyme V44A/ K157N, at pH 7.4 and 50°C
0.25
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157G
0.25
N6-carboxymethyl-NAD+
mutant enzyme V44A/K157G, at pH 7.4 and 50°C
0.36
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant K157N
0.36
N6-carboxymethyl-NAD+
mutant enzyme K157N, at pH 7.4 and 50°C
0.37
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant wild-type enzyme
0.37
N6-carboxymethyl-NAD+
wild type enzyme, at pH 7.4 and 50°C
0.73
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant I154A
0.73
N6-carboxymethyl-NAD+
mutant enzyme I154A, at pH 7.4 and 50°C
1.5
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant I154A/K157G
1.5
N6-carboxymethyl-NAD+
mutant enzyme I154A/K157G, at pH 7.4 and 50°C
2.3
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G
2.3
N6-carboxymethyl-NAD+
mutant enzyme V44A/I154A/K157G, at pH 7.4 and 50°C
2.9
N6-carboxymethyl-NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A
2.9
N6-carboxymethyl-NAD+
mutant enzyme V44A/ I154A, at pH 7.4 and 50°C
0.015
NAD+
-
pH and temperature not specified in the publication
0.0165
NAD+
-
wild type protein, pH 9.5, 30°C
0.0182
NAD+
-
mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30°C
0.021
NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157G
0.024
NAD+
pH 7.4, 50°C, recombinant wild-type enzyme
0.025
NAD+
pH 7.4, 50°C, recombinant mutant K157N
0.031
NAD+
pH 7.4, 50°C, recombinant mutant K157G
0.039
NAD+
pH 7.4, 50°C, recombinant mutant V44A/K157N
0.051
NAD+
pH 7.9, 50°C, recombinant wild-type enzyme
0.07
NAD+
pH 7.4, 50°C, recombinant mutant V44A
0.088
NAD+
pH 7.4, 50°C, recombinant mutant I154A
0.089
NAD+
-
pH 9.0, 25°C
0.108
NAD+
pH 7.4, 50°C, recombinant mutant I154A/K157G
0.23
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
0.351
NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A
0.38
NAD+
wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme
0.4
NAD+
wild-type, pH 8.9, 55°C
0.4614
NAD+
-
mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C
0.5946
NAD+
-
mutant protein D121A, pH 9.5, 30°C
0.6
NAD+
pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G
0.7
NAD+
mutant F245S, pH 8.9, 55°C
0.81
NAD+
-
pH 10.3, 30°C, recombinant enzyme
1
NAD+
-
pH 10.3, 30°C, recombinant enzyme, in presence of 30 mM NH4Cl
1.12
NAD+
Mg-GDH, pH 12.0, 45°C, recombinant enzyme
1.5
NAD+
mutant D121N, pH 8.9, 55°C
2.3
NAD+
mutant /D121NF245S, pH 8.9, 55°C
2.6
NAD+
at pH 8.6 and 35°C
3.2
NAD+
-
pH 10.3, 30°C, recombinant enzyme, in presence of 20 mM KCl
4.07
NAD+
-
pH 9.7, 37°C, wild-type enzyme
4.7
NAD+
-
pH 9.7, 37°C, mutant D
0.005
NADH
-
pH and temperature not specified in the publication
0.02
NADH
pH 7.9, 50°C, recombinant wild-type enzyme
0.05
NADH
-
pH 6.5, 30°C, recombinant enzyme
0.05
NADH
wild-type, pH 5.4, 55°C
0.0513
NADH
recombinant chimeric enzyme GDH-NOX, pH 11.0, 37°C
0.06
NADH
-
pH 6.0, 60°C, recombinant enzyme
0.07
NADH
-
pH 6.5, 30°C, recombinant enzyme, in presence of 20 mM KCl
0.08
NADH
-
pH 9.1, 37°C, wild-type enzyme
0.08
NADH
-
pH 6.5, 30°C, recombinant enzyme, in presence of 30 mM NH4Cl
0.1
NADH
mutant D121N, pH 5.4, 55°C
0.1
NADH
mutant F245S, pH 5.4, 55°C
0.12
NADH
-
pH 9.1, 37°C, mutant D
0.3
NADH
mutant /D121NF245S, pH 5.9, 55°C
54.5
pyruvate
mutant F245S, pH 5.4, 55°C
55.5
pyruvate
mutant /D121NF245S, pH 5.9, 55°C
60.5
pyruvate
mutant D121N, pH 5.4, 55°C
207
pyruvate
wild-type, pH 5.4, 55°C
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
-
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A15T/D16G/V17A/N19K/E23D/Q45E/S46E/T47M/V48L/E49R/F52L/K53A/V58A/V59A/Q70H/D74N/G78D/E81G/T82N/Q83K/G86T/I88V/G108N/R139S/L142M/N145R/K155Q/V256I/L260M
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D121A
-
D121 can potentially hinder the proper binding of substrate 1,3-butanediol due to steric hindrance
D16N/N19A/E23D/L28M/E30N/R31N/Q45E/S46E/V48L/E49R/F52L/K53T/D54G/V58S/G78V/I79V/T82K/A83S/I88V/G108N/R139S/L142M/N145R/K155Q/L211I/G248S/V256I/H268Y/D317E/P319L
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/D121A/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae) and site-directed mutation D121A
Q70H/D74N/G78D/E81G/T82N/Q83K/C84Y/G86T/I88V/G108N/E134A/E204K/L211I/E215K/I234V/V256I/L260M/E291D/S300C/A302S/E316G/V318I/A320T/I324L/T344D/P345S
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
Q70H/G193C/E291Q/A310T
-
mutant selected from a DNA shuffling library (Escherichia coli, Salmonella enterica, Klebsiella pneumoniae)
D123N
mutation abolishes the oxidative activity. The carboxylate of D123 is the base needed for abstracting the proton to form the alkoxy intermediate that precedes the hydride transfer to the nicotinamide cofactor
S305C
-
S305C mutant used for crystallisation
V131A
about 70% of wild-type activity with glycerol
Y142A
mutation reduces the enzyme activity to less than 10% of wild-type activity
I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/I154A
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/K157N
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
I154A
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
K157N
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
D121N
mutation lowers the activity of the enzyme with most all the tested substrates relative to the native enzyme
D121N/F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
F245S
mutant acquires D-lactate dehydrogenase activiy, the alteration increases the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate
L252A
mutation reduces the enzyme activity to less than 10% of wild-type activity and sculpts the active site to accommodate a productive configuration of 3-monoalkyl glycerols
L252A
the mutation sculpts the active site to accommodate a productive configuration of 3-monoalkyl glycerols. This mutation enhances the kcat 163-fold towards 3-ethoxypropan-1,2-diol, resulting in a specific activity similar to the one found for the wild-type towards glycerol. No activity with 3-phenoxypropane-1,2-diol
V44A/K157G
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
V44A/K157G
site-directed mutagenesis, wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold
V44A/K157G
-
site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
-
V44A/K157G
-
site-directed mutagenesis, wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold
-
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, coexpression of all enzymes in Escherichia coli strain BL21(DE3)
additional information
bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250650 nm are prepared that exhibit a 1.4fold enhancement catalytic efficiency. The oligomeric GDH assemblies are coated and stabilized by the excessive manganese-chelated PEIs, which further prevents the disassociation of the GDH subunits, metal-mediated oligomeric assemblies of the enzyme. Half-life of immobilized GDH is enhanced by 5.6folds in aqueous phase at 85°C. Formation of multi-level interactions in the PEI-metal-GDH complex, mechanism, overview. A potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation, and high stability. The activity of PEI-Mn2+-GDH gradually decreases over 5 cycles. PEI-Mn2+-GDH retains 71% and 53% of its initial activity after cycling through 3 and 5 successive reactions, respectively. The decrease in the activity of the recycled catalyst may be due to the leakage of GDH
additional information
the glycerol dehydrogenase gene from Klebsiella pneumoniae is fused to codon-optimized NADH oxidase gene from Lactobacillus brevis. Gene fusion of glycerol dehydrogenase (GDH) and NOX forms a bifunctional multienzyme for bioconversion of glycerol coupled with coenzyme regeneration
additional information
-
the glycerol dehydrogenase gene from Klebsiella pneumoniae is fused to codon-optimized NADH oxidase gene from Lactobacillus brevis. Gene fusion of glycerol dehydrogenase (GDH) and NOX forms a bifunctional multienzyme for bioconversion of glycerol coupled with coenzyme regeneration
-
additional information
-
bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250650 nm are prepared that exhibit a 1.4fold enhancement catalytic efficiency. The oligomeric GDH assemblies are coated and stabilized by the excessive manganese-chelated PEIs, which further prevents the disassociation of the GDH subunits, metal-mediated oligomeric assemblies of the enzyme. Half-life of immobilized GDH is enhanced by 5.6folds in aqueous phase at 85°C. Formation of multi-level interactions in the PEI-metal-GDH complex, mechanism, overview. A potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation, and high stability. The activity of PEI-Mn2+-GDH gradually decreases over 5 cycles. PEI-Mn2+-GDH retains 71% and 53% of its initial activity after cycling through 3 and 5 successive reactions, respectively. The decrease in the activity of the recycled catalyst may be due to the leakage of GDH
-
additional information
-
recombinant co-overexpression of enzymes glycerol dehydrogenase, malate dehydrogenase, and fumarate hydratase from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 12657 in Propionibacterium jensenii leads to increased increased propionic acid production. The transcription levels of the corresponding enzymes in the engineered strains are 2.85 to 8.07fold higher than those in the wild type. The coexpression of GDH and MDH increases the propionic acid titer from 26.95 g/liter in wild-type to 39.43 g/liter in the engineered strains. Fed-batch culture kinetics of propionic acid production from glycerol, overview
additional information
-
recombinant co-overexpression of enzymes glycerol dehydrogenase, malate dehydrogenase, and fumarate hydratase from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 12657 in Propionibacterium jensenii leads to increased increased propionic acid production. The transcription levels of the corresponding enzymes in the engineered strains are 2.85 to 8.07fold higher than those in the wild type. The coexpression of GDH and MDH increases the propionic acid titer from 26.95 g/liter in wild-type to 39.43 g/liter in the engineered strains. Fed-batch culture kinetics of propionic acid production from glycerol, overview
-
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