Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
(2,2-dimethyl-1,3-dioxolan-4-yl)methanol + NADP+
2,2-dimethyl-1,3-dioxolane-4-carbaldehyde + NADPH
-
oxidation reaction. Specific activity: 0.03 micromol/min/mg
-
-
?
(2E)-pent-2-enal + NADPH + H+
(2E)-pent-2-enol + NADP+
-
reduction reaction: specific activity: 4.9 micromol/min/mg. Oxidation reaction specific activity: 0.74 micromol/min/mg
-
-
?
(2R)-2,4-dihydroxybutanal + NADPH + H+
(2R)-2,4-dihydroxybutanol + NADP+
-
reduction reaction. Specific activity: 46.6 micromol/min/mg
-
-
?
(2R,3S)-butane-1,2,3,4-tetrol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.75 micromol/min/mg
-
-
?
(2R,3S,4R,5S)-hexane-1,2,3,4,5,6-hexol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 1.08 micromol/min/mg
-
-
?
(2R,3S,4S)-pentane-1,2,3,4,5-pentol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.25 micromol/min/mg
-
-
?
(2R,4S)-pentane-1,2,3,4,5-pentol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 2.46 micromol/min/mg
-
-
?
(2S)-2,4-dihydroxybutanal + NADPH + H+
(2S)-2,4-dihydroxybutanol + NADP+
-
reduction reaction. Specific activity: 2.0 micromol/min/mg
-
-
?
(2S,3S)-butane-1,2,3,4-tetrol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.9 micromol/min/mg
-
-
?
1,3-dihydroxypropan-2-one + NADPH + H+
propane-1,2,3-triol + NADP+
-
reduction reaction. Specific activity: 0.5 micromol/min/mg
-
-
?
1-phenylethane-1,2-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.77 micromol/min/mg
-
-
?
1-phenylethanone + NADPH + H+
1-phenylethanol + NADP+
-
reduction reaction. Specific activity: 0.04 micromol/min/mg
-
-
?
1-phenylpropanone + NADPH + H+
1-phenylpropanol + NADP+
-
reduction reaction. Specific activity: 0.03 micromol/min/mg
-
-
?
2,3-butanedione + NADPH
?
2,4-difluorobenzaldehyde + NADPH + H+
(2,4-difluorophenyl)methanol + NADP+
-
reduction reaction. Specific activity: 19.6 micromol/min/mg
-
-
?
2,4-dihydroxybutanal + NADPH + H+
2,4-dihydroxybutanol + NADP+
-
reduction reaction. Specific activity: 39.1 micromol/min/mg
-
-
?
2-butenal + NADPH
2-buten-1-ol + NADP+
-
-
-
-
?
2-methylbutanal + NADPH + H+
2-methylbutanol + NADP+
-
reduction reaction. Specific activity: 26.8 micromol/min/mg
-
-
?
2-methylpentanal + NADPH + H+
2-methylpentanol + NADP+
-
reduction reaction. Specific activity: 25.7 micromol/min/mg
-
-
?
2-methylpropanal + NADPH + H+
2-methylpropanol + NADP+
-
reduction reaction. Specific activity: 6.7 micromol/min/mg
-
-
?
3-methylbutanal + NADPH
3-methylbutanol + NADP+
-
-
-
-
?
4-methoxybenzaldehyde + NADPH + H+
(4-methoxyphenyl)methanol + NADP+
-
reduction reaction. Specific activity: 0.3 micromol/min/mg
-
-
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzylalcohol + NADP+
-
-
-
-
?
6-methylheptane-2,5-dione + NADPH + H+
? + NADP+
-
reduction reaction. Specific activity: 0.03 micromol/min/mg
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
-
reduction reaction. Specific activity: 13.8 micromol/min/mg
-
-
?
benzaldehyde + NADPH + H+
benzylalkohol + NADP+
-
-
-
-
?
butanal + NADPH + H+
butanol + NADP+
butane-1,2,4-triol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 1.21 micromol/min/mg
-
-
?
butane-1,2-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.66 micromol/min/mg
-
-
?
butane-1,3-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.04 micromol/min/mg
-
-
?
butane-1,4-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.21 micromol/min/mg
-
-
?
D-erythrose + NADPH
erythritol + NADP+
-
-
-
-
?
D-glucose + NADPH
sorbitol + NADP+
-
-
-
-
?
D-glucuronate + NADP+
?
-
-
-
-
?
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
D-xylose + NADPH
xylitol + NADP+
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
significant enantioselectivity
-
-
r
dodecanal + NADPH + H+
dodecanol + NADP+
-
reduction reaction. Specific activity: 19.3 micromol/min/mg
-
-
?
ethane-1,1-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.5 micromol/min/mg
-
-
?
formaldehyde + NADPH
methanol + NADP+
glycerol + NADP+
? + NADPH + H+
-
oxidation reaction. Specific activity: 0.17 micromol/min/mg
-
-
?
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
dihydroxyacetone + NADPH + H+
glycolaldehyde + NADPH
ethyleneglycol + NADP+
hexan-2-ol + NADP+
hexan-2-one + NADPH
-
oxidation reaction. Specific activity: 0.22 micromol/min/mg
-
-
?
hexanal + NADPH + H+
hexanol + NADP+
hexane-1,2,3-triol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.76 micromol/min/mg
-
-
?
hexane-1,2,6-triol + NADP+
? + NADPH
hexane-1,6-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.87 micromol/min/mg
-
-
?
isobutyraldehyde + NADPH + H+
isobutanol + NADP+
-
-
-
-
?
L-arabitol + NADP+
? + NADPH
-
oxidation reaction
-
-
?
L-glyceraldehyde + NADPH
glycerol + NADP+
methanediol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.05 micromol/min/mg
-
-
?
methylglyoxal + NADPH
1-hydroxyacetone + NADP+
n-butyraldehyde + NADPH
n-butanol + NADP+
n-hexanal + NADPH + H+
n-hexanol + NADP+
-
-
-
-
?
n-pentanal + NADPH + H+
n-pentanol + NADP+
nonanal + NADPH + H+
nonanol + NADP+
-
reduction reaction. Specific activity: 15.9 micromol/min/mg
-
-
?
octan-3-one + NADPH + H+
octan-3-ol + NADP+
-
reduction reaction. Specific activity: 0.02 micromol/min/mg
-
-
?
octanal + NADPH + H+
octanol + NADP+
-
reduction reaction. Specific activity: 35.5 micromol/min/mg
-
-
?
pentane-1,2-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.39 micromol/min/mg
-
-
?
pentane-1,5-diol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.59 micromol/min/mg
-
-
?
propanal + NADPH + H+
propanol + NADP+
-
reduction reaction. Specific activity: 1.1 micromol/min/mg
-
-
?
propionaldehyde + NADPH
propanol + NADP+
additional information
?
-
2,3-butanedione + NADPH
?
-
-
-
-
?
2,3-butanedione + NADPH
?
-
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
reduction reaction. Specific activity: 0.1 micromol/min/mg
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
-
?
butanal + NADPH + H+
butanol + NADP+
-
-
-
-
?
butanal + NADPH + H+
butanol + NADP+
-
reduction reaction. Specific activity: 23.3 micromol/min/mg
-
-
?
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
?
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
enzyme favors reduction reaction
-
-
?
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
diacetyl + NADPH
?
-
-
-
-
?
diacetyl + NADPH
?
-
-
-
-
?
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
r
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
r
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
r
dihydroxyacetone + NADPH
glycerol + NADP+
-
43% of D-glyceraldehyde activity
-
-
r
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
r
dihydroxyacetone + NADPH
glycerol + NADP+
-
-
-
-
r
erythritol + NADP+
?
-
-
-
-
?
erythritol + NADP+
?
-
-
-
-
?
formaldehyde + NADPH
methanol + NADP+
-
-
-
-
?
formaldehyde + NADPH
methanol + NADP+
-
-
-
-
?
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
significant enantioselectivity
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
the reverse reaction is energetically more favorable
-
-
r
glycerol + NADP+
dihydroxyacetone + NADPH + H+
-
-
-
r
glycerol + NADP+
dihydroxyacetone + NADPH + H+
The enzyme plays a role in the glycerol biosynthesis during growth and in osmotolerance. The glycerol biosynthesis by enzyme is required for germination at high osmolarity.
-
-
r
glycolaldehyde + NADPH
ethyleneglycol + NADP+
-
-
-
-
?
glycolaldehyde + NADPH
ethyleneglycol + NADP+
-
-
-
-
?
hexanal + NADPH + H+
hexanol + NADP+
-
-
-
-
?
hexanal + NADPH + H+
hexanol + NADP+
-
reduction reaction. Specific activity: 31.9 micromol/min/mg
-
-
r
hexane-1,2,6-triol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.3 micromol/min/mg
-
-
?
hexane-1,2,6-triol + NADP+
? + NADPH
-
oxidation reaction. Specific activity: 0.45 micromol/min/mg
-
-
?
L-glyceraldehyde + NADPH
glycerol + NADP+
-
36% of D-glyceraldehyde activity
-
-
?
L-glyceraldehyde + NADPH
glycerol + NADP+
-
-
-
-
?
methylglyoxal + NADPH
1-hydroxyacetone + NADP+
-
-
-
-
?
methylglyoxal + NADPH
1-hydroxyacetone + NADP+
-
-
-
-
?
methylglyoxal + NADPH
1-hydroxyacetone + NADP+
-
-
-
-
?
n-butyraldehyde + NADPH
n-butanol + NADP+
-
-
-
-
?
n-butyraldehyde + NADPH
n-butanol + NADP+
-
-
-
-
?
n-pentanal + NADPH + H+
n-pentanol + NADP+
-
-
-
-
?
n-pentanal + NADPH + H+
n-pentanol + NADP+
-
-
-
-
?
propionaldehyde + NADPH
propanol + NADP+
-
-
-
-
?
propionaldehyde + NADPH
propanol + NADP+
-
-
-
-
?
additional information
?
-
-
the enzyme is part of the biosynthetic pathway for glycerol
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
no substrates: D-fructose, D-ribose, D-xylose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
dihydroxyacetone + NADPH + H+
The enzyme plays a role in the glycerol biosynthesis during growth and in osmotolerance. The glycerol biosynthesis by enzyme is required for germination at high osmolarity.
-
-
r
additional information
?
-
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
D-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
glycerol + NADP+
D-glyceraldehyde + NADPH + H+
-
-
-
-
r
additional information
?
-
-
the enzyme is part of the biosynthetic pathway for glycerol
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
additional information
?
-
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
-
-
?
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.
0.04 - 32.3
D-glyceraldehyde
193
L-arabitol
-
oxidation, pH 9.7, 37°C, Vmax: 8.67 micromol/min/mg
additional information
additional information
-
0.04
D-glyceraldehyde
-
-
0.15
D-glyceraldehyde
-
-
2.69
D-glyceraldehyde
-
reduction, pH 7.0, 30°C, Vmax: 77.9 micromol/min/mg
11.5
D-glyceraldehyde
-
-
12.8
D-glyceraldehyde
-
reverse reaction, pH 6.5, 25°C, crude extract
20.2
D-glyceraldehyde
-
reverse reaction, pH 6.5, 25°C, crude extract
32.3
D-glyceraldehyde
-
reverse reaction, pH 6.5, 25°C, crude extract
10
glycerol
-
-
0.0125
NADP+
-
-
0.02
NADP+
-
oxidation, pH 9.7, 37°C, Vmax: 2.1 micromol/min/mg
0.0041
NADPH
wild-type protein, pH 7.0, 30°C
0.0062
NADPH
W23A mutant protein, pH 7.0, 30°C
0.0062
NADPH
W23M mutant protein, pH 7.0, 30°C
0.04
NADPH
-
reduction, pH 7.0, 30°C, Vmax: 101 micromol/min/mg
additional information
additional information
KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C
-
additional information
additional information
-
KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C
-
additional information
additional information
KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C
-
additional information
additional information
-
KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C
-
additional information
additional information
KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C
-
additional information
additional information
-
KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C
-
additional information
additional information
-
enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
-
additional information
additional information
-
enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
-
additional information
additional information
-
enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
-
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.
0.0043
-
cell-free enzyme extract, reverse reaction, pH 6.5, 25°C
0.0049
-
cell-free enzyme extract, reverse reaction, pH 6.5, 25°C
0.0131
-
cell-free enzyme extract, reverse reaction, pH 6.5, 25°C
0.259
-
during growth on wheat grains at water activity at the time of harvest 1.00
0.517
-
during growth on wheat grains at water activity at the time of harvest 0.97
0.582
-
during growth on wheat dough at water activity at the time of harvest 0.98
1.034
-
during growth on wheat dough at water activity at the time of harvest 0.96
22.3
-
glyceraldehyde, crude extract of expressing Escherichia coli, pH not specified in the publication, temperature not specified in the publication
37
W23M mutant protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C
4.2
W23A mutant protein, NADPH as variable substrate, pH 7.0, 30°C
4.9
W23A mutant protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C
54
W23M mutant protein, NADPH as variable substrate, pH 7.0, 30°C
80.5
wild-type protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C
87.1
wild-type protein, NADPH as variable substrate, pH 7.0, 30°C
additional information
comparison of activity in the wild-type and two gldB disruption strains. The presence of 1 M NaCl results in a significant increase in activity in the wild-type strain. In the gldB disruptions hardly any activity is detected.
additional information
-
comparison of activity in the wild-type and two gldB disruption strains. The presence of 1 M NaCl results in a significant increase in activity in the wild-type strain. In the gldB disruptions hardly any activity is detected.
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.
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
-
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
-
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
-
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
-
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
-
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
-
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.
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.
Flynn, T.G.; Cromlish, J.A.
Glycerol dehydrogenase from rabbit muscle
Methods Enzymol.
89
237-242
1982
Oryctolagus cuniculus
brenda
Castro, I.M.; Loureiro-Dias, M.C.
Glycerol utilization in Fusarium oxysporum var. lini: regulation of transport and metabolism
J. Gen. Microbiol.
137
1497-1502
1991
Fusarium oxysporum
brenda
Viswanath-Reddy, M.; Pyle, J.E.; Branch Howe, E.
Purification and properties of NADP+ -linked glycerol dehydrogenase from Neurospora crassa
J. Gen. Microbiol.
107
289-296
1978
Neurospora crassa
-
brenda
Kormann, A.W.; Hurst, R.O.; Flynn, T.G.
Purification and properties of an NADP+ -dependent glycerol dehydrogenase from rabbit skeletal muscle
Biochim. Biophys. Acta
258
40-55
1972
Oryctolagus cuniculus
brenda
Toews, C.J.
The kinetics and reaction mechanism of the nicotinamide-adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle
Biochem. J.
105
1067-1073
1967
Rattus norvegicus
brenda
Walton, D.J.
Stereochemistry of reduction of D-glyceraldehyde catalyzed by a nicotinamide adenine dinucleotide phosphate dependent dehydrogenase from skeletal muscle
Biochemistry
12
3472-3478
1973
Oryctolagus cuniculus
brenda
Schuurink, R.; Busink, R.; Hondmann, D.H.A.; Witteveen, C.F.B.; Visser, J.
Purification and properties of NADP(+)-dependent glycerol dehydrogenases from Aspergillus nidulans and A. niger
J. Gen. Microbiol.
136
1043-1050
1990
Aspergillus nidulans, Aspergillus niger
brenda
Inayat, M.S.; Mattey, M.
Regulation of NADP+-specific glycerol dehydrogenase in Aspergillus niger by bicarbonate ions
Biochem. Soc. Trans.
16
976-977
1988
Aspergillus niger
-
brenda
Sealy-Lewis H.M.; Fairhurst V.
An NADP+-dependent glycerol dehydrogenase in Aspergillus nidulans is inducible by D-galacturonate
Curr. Genet.
22
293-296
1992
Aspergillus nidulans
brenda
Ruijter, G.J.G.; Visser, J.; Rinzema, A.
Polyol accumulation by Aspergillus oryzae at low water activity in solid-state fermentation
Microbiology
150
1095-1101
2004
Aspergillus oryzae
brenda
de Vries, R.P.; Flitter, S.J.; van de Vondervoort, P.J.; Chaveroche, M.K.; Fontaine, T.; Fillinger, S.; Ruijter, G.J.; d'Enfert, C.; Visser, J.
Glycerol dehydrogenase, encoded by gldB is essential for osmotolerance in Aspergillus nidulans
Mol. Microbiol.
49
131-141
2003
Aspergillus nidulans (Q7Z8L1), Aspergillus nidulans
brenda
Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Weckbecker, A.; Eggert, T.; Hummel, W.
Characterization of a whole-cell catalyst co-expressing glycerol dehydrogenase and glucose dehydrogenase and its application in the synthesis of L-glyceraldehyde
Biotechnol. Bioeng.
106
541-552
2010
Gluconobacter oxydans
brenda
Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Eggert, T.; Hummel, W.
Characterisation of a recombinant NADP-dependent glycerol dehydrogenase from Gluconobacter oxydans and its application in the production of L-glyceraldehyde
ChemBioChem
10
1888-1896
2009
Gluconobacter oxydans
brenda
Richter, N.; Breicha, K.; Hummel, W.; Niefind, K.
The Three-Dimensional Structure of AKR11B4, a Glycerol Dehydrogenase from Gluconobacter oxydans, Reveals a Tryptophan Residue as an Accelerator of Reaction Turnover
J. Mol. Biol.
404
353-362
2010
Gluconobacter oxydans (Q5FQJ0), Gluconobacter oxydans
brenda
Rivaldi, J.; Sousa Silva, M.; Duarte, L.; Ferreira, A.; Cordeiro, C.; De Almeida Felipe, M.; De Ponces Freire, A.; De Mancilha, I.
Metabolism of biodiesel-derived glycerol in probiotic Lactobacillus strains
Appl. Microbiol. Biotechnol.
97
1735-1743
2013
Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lactobacillus delbrueckii, Lactiplantibacillus plantarum ATCC 8014, Lactobacillus delbrueckii UFV-H2B20, Lactobacillus acidophilus ATCC 4356
brenda
Roy, S.; Saha, B.; Gupta Bhattacharya, S.
Identifying novel allergens from a common indoor mould Aspergillus ochraceus
J. Proteomics
238
104156
2021
Aspergillus ochraceus
brenda