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evolution

-
the enzyme belongs to the medium-chain dehydrogenase/reductase, MDRase, superfamily
evolution
-
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
evolution
-
the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
evolution
-
NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes; the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes
evolution
-
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
-
evolution
-
the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
-
metabolism

-
in Escherichia coli, the enzyme catalyzes the first step in fermentative glycerol metabolism to produce dihydroxyacetone, biochemical transformation pathway of glycerol, overview
metabolism
-
glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
metabolism
-
glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
-
physiological function

-
GroDHase is mainly involved in Gro utilization as a carbon and energy source
physiological function
-
glycerol dehydrogenase is the enzyme responsible for the oxidation of glycerol to dihydroxyacetone. This permits its entrance into the glycolytic pathway
physiological function
-
glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
physiological function
-
glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
-
additional information

-
protein structure-function relationships
additional information
-
molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
additional information
-
mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis, overview. The binding energy of enzyme ternary complex for Mn-GDH and GDH derived from kinetic parameters indicates that metal ion substitution accelerates the release of dioxyacetone. The metal ion plays a role in catalysis enhancement
additional information
-
molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
-
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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-hydroxybutane-2-one + NADH
-
-
-
r
1,2-butanediol + NAD+
? + NADH
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-chloro-2,3-propanediol + NAD+
?
1-phenylethan-1,2-diol + NAD+
? + NADH
-
-
-
-
?
2,3-butanediol + NAD+
3-hydroxybutane-2-one + NADH
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-chloro-1,2-propanediol + NAD+
?
-
130% of the activity with glycerol
-
-
?
3-hydroxypropionaldehyde + NADH
propan-1,3-diol + NAD+
-
-
-
-
?
3-mercapto-1,2-propanediol + NAD+
?
-
155% of the activity with glycerol
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
acetoin + NADH + H+
2,3-butanediol + NAD+
beta-glycerophosphate + NAD+
?
-
relative activity is 2% compared to oxidation of glycerol
-
-
?
butane-1,3-diol + NAD+
? + NADH
-
-
-
-
?
diglycerol + NAD+
?
-
relative activity is 21% compared to oxidation of glycerol
-
-
?
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
-
-
?
glycerol + NAD+
D-glyceraldehyde + NADH
glycerol + NAD+
dihydroxyacetone + NADH
glycerol + NAD+
dihydroxyacetone + NADH + H+
glycerol + NAD+
glycerone + NADH
-
-
-
-
?
glycerol + NAD+
glycerone + NADH + 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
-
-
?
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+
-
-
-
-
?
R-1-amino-2-propanol + NAD+
?
-
33% of the activity with glycerol
-
-
?
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
-
-
-
-
-
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 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-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-chloro-2,3-propanediol + NAD+

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

D-glyceraldehyde + NADH
-
-
-
-
r
glycerol + NAD+
D-glyceraldehyde + NADH
-
-
-
-
r
glycerol + NAD+

dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
-
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
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
-
the reaction is performed in reverse micelles harboring glycerol and NAD+ in a solution of isooctane containing 250 mM diocytlsulfosuccinate
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
-
-
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+

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+
-
-
-
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+
-
-
-
-
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+
-
-
-
-
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 + 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+
-
-
-
?
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
?
-
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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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 60°C and 70°C
Na+
-
oxidation and reduction slightly increased
K+

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

-
oxidation slightly increased
Mn2+

-
1 mM, activates
Mn2+
-
improvement of activity by the substitution of a zinc ion with a manganese ion, accelerating the release of dioxyacetone; 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+
-
activates, polyethyleneimines-immobilized enzyme PEI-Mn2+-GDH exhibits a 2.9fold increase in activity compared with free GDH
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+

-
1.6 mol Zn2+ bound per subunit
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; 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+
-
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
additional information

-
comparison of the binding energy of enzyme ternary complex for Mn-GDH and Zn-GDH; 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
additional information
-
enzyme inhibition simulations, overview
-
1,10-phenanthroline

-
-
1,10-phenanthroline
-
1 mM
2,2'-bipyridyl

-
-
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

-
-
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
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0.06 - 0.202
1,2-propanediol
11.9 - 77.8
1,3-butanediol
0.0238
2,3-Butanediol
-
-
180
3-amino-1,2-propanediol
-
pH 8.8, 25°C
6.1
3-bromo-1,2-propanediol
-
pH 8.8, 25°C
6
3-Chloro-1,2-propanediol
-
pH 8.8, 25°C
4
3-mercapto-1,2-propanediol
-
pH 8.8, 25°C
0.06 - 4.87
dihydroxyacetone
4.4
R-1-amino-2-propanol
-
pH 8.8, 25°C
500
S-1-amino-2-propanol
-
pH 8.8, 25°C
additional information
additional information
-
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
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
2
dihydroxyacetone
-
pH 9.1, 37°C, mutant D
4.87
dihydroxyacetone
-
-
0.5
glycerol

-
pH 10.0
0.8
glycerol
-
pH 10, 35°C
1.4
glycerol
-
pH 9.0, 25°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
47
glycerol
-
pH 10.3, 30°C, recombinant enzyme, in presence of 20 mM KCl
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
91.7
glycerol
-
pH 9.7, 37°C, wild-type enzyme
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-CM-NAD+

-
pH 7.4, 50°C, recombinant mutant K157G
0.15
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant V44A
0.186
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant V44A/K157N
0.25
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant V44A/K157G
0.36
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant K157N
0.37
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant wild-type enzyme
0.73
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant I154A
1.5
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant I154A/K157G
2.3
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G
2.9
N6-CM-NAD+
-
pH 7.4, 50°C, recombinant mutant V44A/I154A
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
0.4614
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
0.81
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
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
0.014
NADH

-
-
0.02
NADH
-
pH 7.9, 50°C, recombinant wild-type enzyme
0.05
NADH
-
pH 6.5, 30°C, recombinant enzyme
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
0.12
NADH
-
pH 9.1, 37°C, mutant D
additional information
additional information

-
kinetic study with different effectors, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, cooperative behavior of TmGlyDH
-
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; 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
-
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CglD, GST-tagged protein, expressed in E. coli BL21 (DE3)
-
cloning from contaminating bacteria, DNA and amino acid sequence determmination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli train BL21(DE3)pLysS
-
coexpression of enzymes recombinant glycerol dehydrogenase from Escherichia coli, lactate dehydrogenase form Bacillus subtilis, and NADH oxidase LpNox1 from Lactobacillus pentosus in Escherichia coli strain BL21(DE3). The activities of LDH, LpNox1 and GlyDH in the cell-free extract are 98.8, 27.8 and 39.5 U/ml, respectively, overview
-
expressed in Klebsiella pneumoniae KG1
-
expressed in Klebsiella pneumoniae KG1; overexpressed in Klebsiella pneumoniae KG1
-
expression as His-tag fusion protein in Escherichia coli BL21 (DE3) pLysS; gene gld, expression of His-tagged enzyme in strain BL21(DE3)
-
expression in Saccharomyces cerevisiae
-
gene gldA from Escherichia coli strain JM109, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli TOP10 cells
-
gene gldA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)
-
gene gldA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene gldA, recombinant expression in Escherichia coli strain BL21(DE3); gene gldA, recombinant expression in Escherichia coli strain BL21(DE3)
-
gene gldA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
His-tag, expressed in E. coli JM109; His-tagged version
-
His-tagged version expressed in Escherichia coli BL21 STAR (DE3); N-terminal His-tag, expressed in E. coli BL21 STAR (DE3)
His-tagged version expressed in Escherichia coli BL21(DE3)
overexpressed in Schizosaccharomyces pombe
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, quantittive reverse transcription PCR expression analysis
-
recombinant expression of the His-tagged enzyme encoding gene fused to the codon-optimized NADH oxidase gene nox from Lactobacillus brevis, chimeric enzyme GDH-NOX, in Escherichia coli strain BL21(DE3) resulting in bioconversion of glycerol to dihydroxyacetone in the cells
-
recombinent expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pET-32a
-
His-tagged version expressed in Escherichia coli BL21(DE3)

-
His-tagged version expressed in Escherichia coli BL21(DE3)
-
His-tagged version expressed in Escherichia coli BL21(DE3)
-
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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)
S305C
-
S305C mutant used for crystallisation
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/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; 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/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
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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K157N
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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V44A
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme
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V44A/K157G
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site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme; 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
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additional information

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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
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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
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bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250–650 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
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bioinspired immobilization of glycerol dehydrogenase by metal ion-chelated polyethyleneimines (PEI) as artificial polypeptides. Nanoparticles with diameters from 250–650 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; 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
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additional information
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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
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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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analysis

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glycerol dehydrogenase can be immobilised in a polycarbamoyl sulfonate-hydrogel and used as a sensor for glycerol
analysis
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development of an integrated multienzyme electrochemical biosensor for the determination of glycerol in wines. The biosensor is based on the glycerol dehydrogenase/diaphorase bienzyme system. The enzyme system is immobilized together with the mediator tetrathiafulvalene on a 3-mercaptopropionic acid self-assembled monolayer-modified gold electrode by using a dialysis membrane
analysis
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the recombinant chimeric fusion enzyme GDH-NOX has a potential application for quick glycerol analysis and dioxyacetone biosynthesis
analysis
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the recombinant chimeric fusion enzyme GDH-NOX has a potential application for quick glycerol analysis and dioxyacetone biosynthesis
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biotechnology

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production of 1,2-propanediol in yeast
biotechnology
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GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
biotechnology
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GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
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brewing

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enzymatic assay for the determination of glycerol in wine and beer
brewing
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enzymatic assay for the determination of glycerol in wine and beer
molecular biology

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enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
molecular biology
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enzymatic redox cofactor regeneration in organic media: functionalization and application of recombinant glycerol dehydrogenase and soluble transhydrogenase in reverse micelles, overview
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synthesis

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high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
synthesis
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biotransformation of glycerol to dihydroxyacetone by recombinant Gluconobacter oxydans DSM 2343. Overproduction of the glycerol dehydrogenase to improve production of dihydroxyacetone
synthesis
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Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, heterologous gene GldA is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
synthesis
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GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor
synthesis
-
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 (DHA), no expensive consumption of NAD+ for the production of DHA, overview. DHA is a valuable chemical with a wide range of applications in the cosmetics
synthesis
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high specificity of enzyme for secondary alcohols in R-configuration, use of enzyme for production of chiral compounds
-
synthesis
-
GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor; Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, heterologous gene GldA is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
-
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Klebsiella aerogenes
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Clostridium beijerinckii and Clostridium difficile detoxify methylglyoxal by a novel mechanism involving glycerol dehydrogenase
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-
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