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2-amino-2-deoxy-D-glucose + NAD(P)+
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
2-amino-2-deoxy-D-glucose + NADP+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
5% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-beta-D-xylose + NAD+
2-deoxy-D-xylono-1,5-lactone + NADH + H+
-
-
-
-
r
2-deoxy-D-glucose + NAD(P)+
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
2-deoxy-D-glucose + NAD+
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
2-deoxy-D-glucose 6-phosphate + NAD+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADH
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
6-deoxy-D-glucose + NAD(P)+
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
66% of the activity with D-glucose
-
-
?
6-deoxy-D-glucose + NADP+
? + NADPH
-
9% of the activity with D-glucose and NAD+
-
-
?
beta-D-galactose + NAD+
D-galactono-1,5-lactone + NADH
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
-
-
ir
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
-
-
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
beta-D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
beta-D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
26% activity compared to D-glucose
-
-
r
cellobiose + NAD+
? + NADH
D-allose + NAD(P)+
?
-
low activity
-
-
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
-
8% of the activity with D-glucose
-
-
?
D-allose + NADP+
D-allono-1,5-lactone + NADPH
-
13% of the activity with D-glucose and NAD+
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
-
5% of the activity with D-glucose
-
-
?
D-altrose + NADP+
?
-
low activity
-
-
?
D-altrose + NADP+
D-altrono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-cellobiose + NAD+
? + NADH
-
-
-
-
?
D-fructose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-fructose + NAD+
? + NADH
-
9% of the activity with D-glucose
-
-
?
D-fructose + NADP+
?
-
0.03% activity compared to D-glucose
-
-
?
D-fucose + NAD(P)+
?
-
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
D-galactose + NADP+
?
-
1.09% activity compared to D-glucose
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
D-galactose 6-phosphate + NAD+
6-phospho-D-galactono-1,5-lactone + NADH + H+
-
-
-
-
r
D-galactose 6-phosphate + NADP+
6-phospho-D-galactono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucosamine + NAD(P)+
?
low activity
-
-
?
D-glucosamine + NAD+
?
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
D-glucosamine + NADP+
D-glucosamino-1,5-lactone + NADPH
-
-
-
-
?
D-glucose + 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
-
-
-
?
D-glucose + 1-benzyl-3-carbamoylpyridin-1-ium chloride
D-glucono-1,5-lactone + reduced 1-benzyl-3-carbamoylpyridin-1-ium chloride
-
-
-
?
D-glucose + 1-phenethyl-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-phenethyl-1,4-dihydropyridine-3-carboxamide
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
D-gulose + NAD(P)+
?
-
low activity
-
-
?
D-gulose + NAD+
D-gulono-1,5-lactone + NADH
-
8% of the activity with D-glucose
-
-
?
D-gulose + NADP+
D-gulono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-idose + NAD(P)+
?
low activity
-
-
?
D-idose + NAD+
D-idono-1,5-lactone + NADH
-
65% of the activity with D-glucose
-
-
?
D-idose + NADP+
D-idono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-lactose + NAD+
D-lactono-1,5-lactone + NADH + H+
relative activity: 4.2%
-
-
?
D-lactose + NADP+
?
-
3.0% activity compared to D-glucose
-
-
?
D-lyxose + NAD(P)+
?
low activity
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
D-maltose + NADP+
?
-
1.03% activity compared to D-glucose
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
D-mannose + NAD+
?
weak substrate
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
D-mannose + NADP+
?
-
11.53% activity compared to D-glucose
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
-
4% of the activity with D-glucose and NADP+
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
D-xylose + NAD+
?
weak substrate
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
D-xylose + NADP+
?
-
12.89% activity compared to D-glucose
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
gentiobiose + NAD+
? + NADH
gluconate + NAD+
? + NADH
maltose + NADP+
? + NADPH
sucrose + NAD+
?
relative activity: 6.3%
-
-
?
additional information
?
-
2-amino-2-deoxy-D-glucose + NAD(P)+
?
-
-
-
-
?
2-amino-2-deoxy-D-glucose + NAD(P)+
?
-
-
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
14% of the activity with D-glucose
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
26% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD(P)+
?
low activity
-
-
?
2-deoxy-D-glucose + NAD(P)+
?
-
low activity
-
-
?
2-deoxy-D-glucose + NAD(P)+
?
-
low activity
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
113% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
113% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
108% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
114% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
112% relative activity
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
112% relative activity
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
12% of the activity with glucose
-
-
?
2-deoxy-D-glucose + NAD+
?
-
-
-
?
2-deoxy-D-glucose + NAD+
?
-
-
-
?
2-deoxy-D-glucose + NAD+
?
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
103% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
103% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
25% of the activity with D-glucose and NAD+
-
-
?
6-deoxy-D-glucose + NAD(P)+
?
-
-
-
?
6-deoxy-D-glucose + NAD(P)+
?
-
-
-
-
?
beta-D-galactose + NAD+
D-galactono-1,5-lactone + NADH
6.8% of the activity as compared to D-glucose
-
-
?
beta-D-galactose + NAD+
D-galactono-1,5-lactone + NADH
6.8% of the activity as compared to D-glucose
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
low activity
-
-
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
best substrate, wild-type and mutant enzymes
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
first step of the non-phosphorylative Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
9% of the activity with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km for glucose in the reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
93% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
93% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
1% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
1% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
in the reverse reaction only 4% of the reaction occurs at neutral pH
-
-
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
-
-
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km of NADP+ is about 8fold higher compared to kcat/Km of NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km of glucose in the reaction with NADP+ is about 8fold higher compared to kcat/Km of glucose in reaction with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100fold higher affinity for NADP+ than for NAD+
-
-
ir
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
cellobiose + NAD+
? + NADH
-
89% of the activity with D-glucose
-
-
?
cellobiose + NAD+
? + NADH
-
as active as glucose
-
-
?
cellobiose + NAD+
? + NADH
-
as active as glucose
-
-
?
cellobiose + NAD+
? + NADH
-
as active as glucose
-
-
?
D-fructose + NAD+
?
weak substrate
-
-
?
D-fructose + NAD+
?
weak substrate
-
-
?
D-fructose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
low activity with wild-type and mutant enzymes
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
equally active compared to beta-D-glucose
-
-
?
D-galactose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD+
?
weak substrate
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
-
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
15% of the activity with D-glucose and NAD+
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
relative activity: 17.3%
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
relative activity: 17.3%
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 2.9% (reference: D-glucose 100%)
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 9.1% (reference: D-glucose 100%)
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
5% of the activity with D-glucose
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
-
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
-
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 11% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 3% (reference: D-glucose 100%)
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
the enzyme prefers NAD+ rather than NADP+
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
the enzyme prefers NAD+ rather than NADP+
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
relative activity: 100%
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
about 20% activity with D-galactose, D-xylose, maltose
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
relative activity: 100%
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
about 20% activity with D-galactose, D-xylose, maltose
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme prefers NAD+ rather than NADP+
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
the enzyme prefers NAD+ rather than NADP+
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100% activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100% activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
75% relative activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
75% relative activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
other substrates: hexose-6-phosphates, glucose-6-sulfate, glucose
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-maltose + NAD+
?
10% of the activity as compared to D-glucose
-
-
?
D-maltose + NAD+
?
10% of the activity as compared to D-glucose
-
-
?
D-maltose + NAD+
?
relative activity: 22.4%
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
-
-
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
-
wild-type and mutant enzymes
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
-
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
2% relative activity
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
2% relative activity
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
relative activity: 7.6%
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 18% (reference: D-glucose 100%)
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 4.8% (reference: D-glucose 100%)
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
88% of the activity with D-glucose
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
-
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
no activity
-
-
?
D-ribose + NADP+
?
-
low activity
-
-
?
D-ribose + NADP+
?
-
low activity
-
-
?
D-xylose + NAD(P)+
?
-
-
-
?
D-xylose + NAD(P)+
?
-
-
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
wild-type and mutant enzymes
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
44% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
44% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
-
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 10% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 35% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
28% of the activity with D-glucose and NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
6.1% of the activity as compared to D-glucose
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
6.1% of the activity as compared to D-glucose
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
28% of the activity with D-glucose and NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
-
-
-
?
gentiobiose + NAD+
? + NADH
-
103% of the activity with gentiobiose
-
-
?
gentiobiose + NAD+
? + NADH
-
86% of the activity with D-glucose
-
-
?
gluconate + NAD+
? + NADH
-
-
-
-
?
gluconate + NAD+
? + NADH
-
-
-
-
?
L-arabinose + NAD(P)+
?
-
-
-
-
?
L-arabinose + NAD(P)+
?
-
-
-
?
maltose + NAD+
? + NADH
-
6% of the activity with D-glucose
-
-
?
maltose + NAD+
? + NADH
-
6% of the activity with D-glucose
-
-
?
maltose + NADP+
? + NADPH
-
5% of the activity D-glucose and NAD+
-
-
?
maltose + NADP+
? + NADPH
-
5% of the activity D-glucose and NAD+
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
Cys residues are not involved in the catalytic site
-
-
?
additional information
?
-
-
no activity of wild-type and mutant enzymes with sucrose
-
-
?
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
?
additional information
?
-
D-ribose, maltose, lactose and sucrose are poor substrates, no activity with D-allose, D-arabinose, and D-mannose
-
-
?
additional information
?
-
no substrates: D-allose, D-mannose, L-arabinose, D-ribose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose, ethanol
-
-
?
additional information
?
-
no substrates: D-allose, D-mannose, L-arabinose, D-ribose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose, ethanol
-
-
?
additional information
?
-
-
broad substrate specificity, no activity with D-mannose, D-ribose, and glucose 6-phosphate, cofactor specificity depends on the sugar sustrate
-
-
?
additional information
?
-
-
broad substrate specificity, no activity with D-mannose, D-ribose, and glucose 6-phosphate, cofactor specificity depends on the sugar sustrate
-
-
?
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3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
11{beta}-Hydroxysteroid Dehydrogenase Type 1: A Tissue-Specific Regulator of Glucocorticoid Response.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
A follow-up history of young man with apparent cortisone reductase deficiency (ACRD) - several years after diagnosis.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
A study of the hexose-6-phosphate dehydrogenase gene R453Q and 11beta-hydroxysteroid dehydrogenase type 1 gene 83557insA polymorphisms in the polycystic ovary syndrome.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Alterations of Cortisol Metabolism in Human Disorders.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Genotypes at 11beta-hydroxysteroid dehydrogenase type 11B1 and hexose-6-phosphate dehydrogenase loci are not risk factors for apparent cortisone reductase deficiency in a large population-based sample.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Hexose-6-phosphate dehydrogenase confers oxo-reductase activity upon 11 beta-hydroxysteroid dehydrogenase type 1.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Hexose-6-phosphate dehydrogenase: a new risk gene for multiple sclerosis.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Lack of Association of the 11beta-hydroxysteroid dehydrogenase type 1 gene 83,557insA and hexose-6-phosphate dehydrogenase gene R453Q polymorphisms with body composition, adrenal androgen production, blood pressure, glucose metabolism, and dementia.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Mutations of the hexose-6-phosphate dehydrogenase gene rarely cause hyperandrogenemic polycystic ovary syndrome.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Novel H6PDH mutations in two girls with premature adrenarche: 'apparent' and 'true' CRD can be differentiated by urinary steroid profiling.
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Steroid biomarkers and genetic studies reveal inactivating mutations in hexose-6-phosphate dehydrogenase in patients with cortisone reductase deficiency.
Dementia
Lack of Association of the 11beta-hydroxysteroid dehydrogenase type 1 gene 83,557insA and hexose-6-phosphate dehydrogenase gene R453Q polymorphisms with body composition, adrenal androgen production, blood pressure, glucose metabolism, and dementia.
Diabetes Mellitus
Adipose tissue 11-beta-Hydroxysteroid Dehydrogenase Type 1 and Hexose-6-Phosphate Dehydrogenase gene expressions are increased in patients with type 2 diabetes mellitus.
Diabetes Mellitus, Type 2
Adipose tissue 11-beta-Hydroxysteroid Dehydrogenase Type 1 and Hexose-6-Phosphate Dehydrogenase gene expressions are increased in patients with type 2 diabetes mellitus.
Diabetes Mellitus, Type 2
Relationship of 11?-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase gene polymorphisms with metabolic syndrome and type 2 diabetes.
Diabetes Mellitus, Type 2
Tissue-specific dysregulation of hexose-6-phosphate dehydrogenase and glucose-6-phosphate transporter production in db/db mice as a model of type 2 diabetes.
Hyperandrogenism
Alterations of Cortisol Metabolism in Human Disorders.
Hyperandrogenism
Mutations of the hexose-6-phosphate dehydrogenase gene rarely cause hyperandrogenemic polycystic ovary syndrome.
Hypoglycemia
Hypoglycemia with enhanced hepatic glycogen synthesis in recombinant mice lacking hexose-6-phosphate dehydrogenase.
Insulin Resistance
Glucocorticoid receptor gene expression in adipose tissue and associated metabolic risk in black and white South African women.
Insulin Resistance
Reduction of hepatic glucocorticoid receptor and hexose-6-phosphate dehydrogenase expression ameliorates diet-induced obesity and insulin resistance in mice.
Insulin Resistance
The R453Q and D151A polymorphisms of Hexose-6-Phosphate Dehydrogenase Gene (H6PD) influence the polycystic ovary syndrome (PCOS) and obesity.
Leukemia
Genetic studies of the Fv-1 locus of mice: linkage with Gpd-1 in recombinant inbred lines.
Metabolic Syndrome
11?-Hydroxysteroid dehydrogenase type 1 shRNA ameliorates glucocorticoid-induced insulin resistance and lipolysis in mouse abdominal adipose tissue.
Metabolic Syndrome
Glucocorticoid metabolism within superficial subcutaneous rather than visceral adipose tissue is associated with features of the metabolic syndrome in South African women.
Metabolic Syndrome
Hexose-6-phosphate dehydrogenase knock-out mice lack 11 beta-hydroxysteroid dehydrogenase type 1-mediated glucocorticoid generation.
Metabolic Syndrome
Hexose-6-phosphate dehydrogenase: linking endocrinology and metabolism in the endoplasmic reticulum.
Metabolic Syndrome
Liver upregulation of genes involved in cortisol production and action is associated with metabolic syndrome in morbidly obese patients.
Metabolic Syndrome
Physiological roles of 11 beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase.
Metabolic Syndrome
Relationship of 11?-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase gene polymorphisms with metabolic syndrome and type 2 diabetes.
Multiple Sclerosis
Hexose-6-phosphate dehydrogenase: a new risk gene for multiple sclerosis.
Muscular Diseases
Deletion of Hexose-6-phosphate Dehydrogenase Activates the Unfolded Protein Response Pathway and Induces Skeletal Myopathy.
Muscular Diseases
Nonimmune mechanisms of muscle damage in myositis: role of the endoplasmic reticulum stress response and autophagy in the disease pathogenesis.
Neoplasms
Hexose-6-phosphate dehydrogenase controls cancer cell proliferation and migration through pleiotropic effects on the unfolded-protein response, calcium homeostasis, and redox balance.
Obesity
Liver upregulation of genes involved in cortisol production and action is associated with metabolic syndrome in morbidly obese patients.
Obesity
Physiological roles of 11 beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase.
Obesity
Reduction of hepatic glucocorticoid receptor and hexose-6-phosphate dehydrogenase expression ameliorates diet-induced obesity and insulin resistance in mice.
Obesity
The R453Q and D151A polymorphisms of Hexose-6-Phosphate Dehydrogenase Gene (H6PD) influence the polycystic ovary syndrome (PCOS) and obesity.
Polycystic Ovary Syndrome
A study of the hexose-6-phosphate dehydrogenase gene R453Q and 11beta-hydroxysteroid dehydrogenase type 1 gene 83557insA polymorphisms in the polycystic ovary syndrome.
Polycystic Ovary Syndrome
Expression of 11beta-hydroxysteroid dehydrogenase 1 and 2 in subcutaneous adipose tissue of lean and obese women with and without polycystic ovary syndrome.
Polycystic Ovary Syndrome
Mutations of the hexose-6-phosphate dehydrogenase gene rarely cause hyperandrogenemic polycystic ovary syndrome.
Polycystic Ovary Syndrome
The Expression of 11?-HSDs, GR, and H6PDH in Subcutaneous Adipose Tissue from Polycystic Ovary Syndrome Subjects.
Polycystic Ovary Syndrome
The R453Q and D151A polymorphisms of Hexose-6-Phosphate Dehydrogenase Gene (H6PD) influence the polycystic ovary syndrome (PCOS) and obesity.
Prostatic Neoplasms
Hexose-6-phosphate dehydrogenase blockade reverses prostate cancer drug resistance in xenograft models by glucocorticoid inactivation.
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2.5 - 12.76
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
-
1.67 - 14.78
1-benzyl-3-carbamoylpyridin-1-ium chloride
-
4.35 - 16.33
1-phenethyl-1,4-dihydropyridine-3-carboxamide
-
47.8
2-deoxy-beta-D-glucose
-
pH 7.8, 23°C
4.2
2-deoxy-D-glucose
-
pH 6.5
0.3 - 25
2-deoxy-D-glucose 6-phosphate
9.8 - 11
4-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
3.2 - 5.6
6-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
0.44 - 204
beta-D-galactose
0.0024 - 135
beta-D-glucose
68
beta-D-xylose
-
pH 9.0, 70°C, coenzyme NAD+
0.04 - 5
D-galactose 6-phosphate
35
D-glucosamine
-
pH 6.5
0.0015 - 0.1
D-glucose 6-phosphate
0.0029 - 0.0083
D-Glucose-6-phosphate
0.01
galactose 6-phosphate
additional information
additional information
-
steady-state kinetic analysis
-
2.5 - 3
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
4.1
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
5.13
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
10.29
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
11.32
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
11.57
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
12.76
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
1.67
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
5.49
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
8.76
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306G
-
10.24
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, wild-type enzyme
-
13.02
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192V
-
13.15
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306I
-
14.78
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T
-
4.35
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
7.07
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
8.16
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
11.84
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
13.87
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
15.26
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
16.33
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
0.3
2-deoxy-D-glucose 6-phosphate
-
pH 7.5, 25°C, coenzyme NAD+
1
2-deoxy-D-glucose 6-phosphate
-
pH 7.5, 25°C, coenzyme NADP+
25
2-deoxy-D-glucose 6-phosphate
-
pH 10, 25°C, coenzyme NADP+
9.8
4-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
-
strain 150-1
11
4-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
-
strain 93-1
3.2
6-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
-
strain 93-1
5.6
6-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
-
strain 150-1
0.44
beta-D-galactose
wild type enzyme, NADP+ as cofactor
0.57
beta-D-galactose
wild type enzyme, NAD+ as cofactor
22
beta-D-galactose
-
pH 9.0, 70°C, coenzyme NADP+
109
beta-D-galactose
mutant enzyme T41A, NADP+ as cofactor
118
beta-D-galactose
mutant enzyme T41A, NAD+ as cofactor
175
beta-D-galactose
mutant enzyme T41V, NADP+ as cofactor
204
beta-D-galactose
mutant enzyme T41V, NAD+ as cofactor
0.0024
beta-D-glucose
-
pH 7.5, 37°C, coenzyme NAD+, 37°C
0.0032
beta-D-glucose
-
pH 10.0, 37°C, coenzyme NAD+
0.011
beta-D-glucose
-
pH 7.5, 37°C, coenzyme NADP+
0.032
beta-D-glucose
-
pH 10.0, 37°C, coenzyme NADP+
0.14
beta-D-glucose
-
reduction, reverse reaction
0.17
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
0.3
beta-D-glucose
-
pH 7.0, 70°C
0.44
beta-D-glucose
-
pH 9.0, 70°C, coenzyme NADP+
1.3
beta-D-glucose
wild type enzyme, NADP+ as cofactor
1.5
beta-D-glucose
wild type enzyme, NAD+ as cofactor
2.2
beta-D-glucose
-
pH 9.0, 70°C, coenzyme NADP+
2.57
beta-D-glucose
-
oxidation, forward reaction
2.7
beta-D-glucose
-
E96K mutant, coenzyme NAD+
2.8
beta-D-glucose
pH 7.0, 70°C
3.38
beta-D-glucose
-
pH 9.5, 30°C, coenzyme NAD+
4
beta-D-glucose
-
E96K mutant, coenzyme NADP+
4.5
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH IV, coenzyme NADP+
4.59
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
4.6
beta-D-glucose
-
pH 9.0
4.6
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH I, coenzyme NAD+
4.8
beta-D-glucose
-
pH 6.5, Km -value decreases with decreasing pH
7.9
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH I, coenzyme NADP+
8
beta-D-glucose
-
pH 9.0, 70°C, coenzyme NAD+
8
beta-D-glucose
-
mutant Q252L, pH 8.0, 25°C
8.5
beta-D-glucose
-
mutant Q252L/E170K, pH 8.0, 25°C
8.7
beta-D-glucose
-
pH 8.0, 25°C
8.7
beta-D-glucose
-
E96A mutant, coenzyme NAD+
9
beta-D-glucose
-
Q252L mutant, coenzyme NAD+
9.2
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH II, coenzyme NAD+
9.5
beta-D-glucose
-
wild type, coenzyme NAD+
9.8
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH IV, coenzyme NAD+
10
beta-D-glucose
-
pH 7.0, 55°C
10
beta-D-glucose
-
Q252L mutant, coenzyme NADP+
11
beta-D-glucose
-
wild type, coenzyme NADP+
12.4
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH II, coenzyme NADP+
13
beta-D-glucose
-
E96A mutant, coenzyme NADP+
14
beta-D-glucose
-
pH 7.5
14
beta-D-glucose
-
wild-type enzyme, pH 8.0, 25°C
15
beta-D-glucose
-
pH 7.5, enzyme reduced with Nostoc sp. thioredoxin
16
beta-D-glucose
-
E96G mutant, coenzyme NAD+
18
beta-D-glucose
-
E96G mutant, coenzyme NADP+
20
beta-D-glucose
-
pH 10, 25°C, coenzyme NAD+
24.8
beta-D-glucose
mutant enzyme T41A, NAD+ as cofactor
33.3
beta-D-glucose
mutant enzyme T41A, NADP+ as cofactor
40
beta-D-glucose
-
pH 10, 25°C, coenzyme NADP+
42.9
beta-D-glucose
-
pH 7.8, 30°C, coenzyme NADP+
44
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH III, coenzyme NAD+
47.22
beta-D-glucose
-
pH 9.5, 30°C, coenzyme NADP+
47.5
beta-D-glucose
-
pH 9.0, 25°C
55
beta-D-glucose
-
Y253C mutant, coenzyme NAD+
55.9
beta-D-glucose
-
pH 7.8, 30°C
59
beta-D-glucose
mutant enzyme T41V, NADP+ as cofactor
70
beta-D-glucose
-
pH 9.9, 30°C
72.5
beta-D-glucose
mutant enzyme T41V, NAD+ as cofactor
85
beta-D-glucose
-
Y253C mutant, coenzyme NADP+
135
beta-D-glucose
-
pH 8.0, 30°C, isoenzyme GlcDH III, coenzyme NADP+
800
D-galactose
-
about, pH 7.5, 25°C, coenzyme NAD+
1000
D-galactose
-
about, pH 10, 25°C, coenzyme NAD+
4000
D-galactose
-
about, pH 10, 25°C, coenzyme NADP+
10000
D-galactose
-
pH 7.5, 25°C, coenzyme NADP+
0.04
D-galactose 6-phosphate
-
pH 7.5, 25°C, coenzyme NAD+
0.04
D-galactose 6-phosphate
-
at pH 7.5 and 25°C
3
D-galactose 6-phosphate
-
pH 10, 25°C, coenzyme NAD+
3
D-galactose 6-phosphate
-
at pH 10.0 and 25°C
5
D-galactose 6-phosphate
-
pH 10, 25°C, coenzyme NADP+
5
D-galactose 6-phosphate
-
at pH 10.0 and 25°C
0.17
D-glucose
cosubstrate NADP+, 70°C, pH not specified in the publication
0.55
D-glucose
-
at pH 9.0 and 55°C
3.1
D-glucose
pH 6.0, 37°C, wild-tpye
4 - 10
D-glucose
pH 6.0, 37°C, mutant G261A
4.3
D-glucose
pH 6.0, 37°C, mutant A258F
4.59
D-glucose
cosubstrate NAD+, 70°C, pH not specified in the publication
5
D-glucose
-
pH 8.0, 25°C
5.1
D-glucose
with NADP+, pH 8.0, 25°C
5.5
D-glucose
-
with NADP+ as cosubstrate,at pH 8.0 and 37°C
6
D-glucose
with NAD+, pH 8.0, 25°C
7.5
D-glucose
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
8
D-glucose
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
8.5
D-glucose
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
9.8
D-glucose
pH 8.0, 37°C, mutant A258F
11
D-glucose
pH 6.0, 37°C, wild-tpye
12
D-glucose
pH 8.0, 37°C, wild-tpye
14
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
14.8
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P
16
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R
16.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R
17.126
D-glucose
pH 8.0, 25°C
17.2
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
17.3
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
17.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K
17.5
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
63
D-glucose
pH 8.0, 37°C, wild-tpye
80
D-glucose
-
pH 7.5, 25°C, coenzyme NADP+
80
D-glucose
-
at pH 7.5 and 25°C
81
D-glucose
pH 6.0, 37°C, mutant G259A
380
D-glucose
pH 8.0, 37°C, mutant G259A
1100
D-glucose
pH 6.0, 37°C, mutant DELTAG261
1400
D-glucose
pH 6.0, 37°C, mutant G259V
2000
D-glucose
pH 8.0, 37°C, mutant DELTAG261
2000
D-glucose
pH 8.0, 37°C, mutant G261A
4000
D-glucose
pH 6.0, 37°C, mutant G261V
4000
D-glucose
pH 8.0, 37°C, mutant G259V
5000
D-glucose
pH 8.0, 37°C, mutant G261V
0.0015
D-glucose 6-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.01
D-glucose 6-phosphate
-
pH 7.5, 25°C, coenzyme NAD+
0.02
D-glucose 6-phosphate
-
pH 7.5, 25°C, coenzyme NADP+
0.0255
D-glucose 6-phosphate
-
coenzyme NADP+
0.049
D-glucose 6-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.1
D-glucose 6-phosphate
-
pH 10, 25°C, coenzyme NAD+ or NADP+
0.0029
D-Glucose-6-phosphate
-
37°C, pH 7.5, coenzyme NADP+
0.0072
D-Glucose-6-phosphate
-
pH 10.0, 37°C, coenzyme NADP+
0.0083
D-Glucose-6-phosphate
-
pH 10.0
0.18
D-xylose
wild type enzyme, NADP+ as cofactor
0.25
D-xylose
wild type enzyme, NAD+ as cofactor
20.4
D-xylose
mutant enzyme T41A, NADP+ as cofactor
29.2
D-xylose
mutant enzyme T41A, NAD+ as cofactor
65.8
D-xylose
mutant enzyme T41V, NADP+ as cofactor
70
D-xylose
-
pH 10, 25°C, coenzyme NAD+
76.3
D-xylose
mutant enzyme T41V, NAD+ as cofactor
80
D-xylose
-
pH 7.5, 25°C, coenzyme NAD+
100
D-xylose
-
pH 7.5, 25°C, coenzyme NADP+
200
D-xylose
-
pH 7.5, 25°C, coenzyme NADP+
0.01
galactose 6-phosphate
-
pH 7.5, 25°C, coenzyme NADP+
0.01
galactose 6-phosphate
-
at pH 7.5 and 25°C
0.0003
NAD+
-
pH 9.9, 30°C
0.0051
NAD+
-
pH 7.5, 37°C, reaction with beta-D-glucose
0.0212
NAD+
-
pH 9.5, 30°C, substrate beta-D-glucose
0.081
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH I
0.088
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH IV
0.094
NAD+
wild type enzyme, at pH 8.0 and 25°C
0.15
NAD+
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.16
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH III
0.17
NAD+
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.17
NAD+
-
at pH 9.0 and 55°C
0.17
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.22
NAD+
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.25
NAD+
-
at pH 8.0 and 37°C
0.293
NAD+
mutant enzyme DS255, at pH 8.0 and 25°C
0.33
NAD+
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.344
NAD+
-
at pH 8.0 and 25°C
0.36
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T
0.41
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.43
NAD+
pH and temperature not specified in the publication, wild-type enzyme
0.47
NAD+
pH and temperature not specified in the publication, mutant enzyme I192V
0.57
NAD+
with beta-D-galactose, pH 7.5, 70°C
0.86
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
0.99
NAD+
-
pH 8.0, 30°C, isoenzyme GlcDH II
1.5
NAD+
with beta-D-glucose, pH 7.5, 70°C
2.23
NAD+
cosubstrate D-glucose, 70°C, pH not specified in the publication
2.64
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
3.3
NAD+
cosubstrate D-glucose, 80°C, pH not specified in the publication
5.59
NAD+
cosubstrate D-glucose, 65°C, pH not specified in the publication
0.0036
NADP+
-
pH 7.5, 37°C, reaction with D-glucose-6-phosphate
0.0046
NADP+
-
pH 10.0, 37°C, reaction with beta-D-glucose
0.0051
NADP+
-
E96K mutant
0.0076
NADP+
-
E96G mutant
0.0093
NADP+
-
E96A mutant
0.01
NADP+
-
pH 8.0, 25°C
0.013
NADP+
-
pH 7.5, 37°C, reaction with beta-D-glucose
0.018
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH II
0.02
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH I
0.026
NADP+
-
Q252L mutant
0.026
NADP+
-
pH not specified in the publication, temperature not specified in the publication
0.028
NADP+
-
pH 10.0, 37°C, reaction with beta-D-glucose
0.03
NADP+
-
pH 9.0, 70°C
0.03
NADP+
-
at pH 9.0 and 55°C
0.037
NADP+
-
Y253C mutant
0.05
NADP+
-
at pH 8.0 and 37°C
0.062
NADP+
-
pH 10.0, 37°C, reaction with D-glucose-6-phosphate
0.062
NADP+
-
pH 9.5, 30°C, reaction with D-glucose 6-phosphate
0.072
NADP+
wild type enzyme, at pH 8.0 and 25°C
0.113
NADP+
-
pH 7.0, 55°C
0.14
NADP+
cosubstrate D-glucose, 70°C, pH not specified in the publication
0.15
NADP+
cosubstrate D-glucose, 65°C, pH not specified in the publication
0.15
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
0.197
NADP+
mutant enzyme DS255, at pH 8.0 and 25°C
0.26
NADP+
-
pH 7.8, 30°C
0.285
NADP+
-
pH 7.5, enzyme reduced with Nostoc sp. thioredoxin
0.44
NADP+
with beta-D-galactose, pH 7.5, 70°C
1.3
NADP+
with beta-D-glucose, pH 7.5, 70°C
1.9
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH IV
18.9
NADP+
-
pH 8.0, 30°C, isoenzyme GlcDH III
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00023 - 0.00697
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
-
0.00078 - 0.009
1-benzyl-3-carbamoylpyridin-1-ium chloride
-
0.00047 - 0.042
1-phenethyl-1,4-dihydropyridine-3-carboxamide
-
1.5 - 14.2
D-glucose 6-phosphate
0.00023
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.00076
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.0009
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.00096
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
0.00126
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.00697
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
0.00078
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.00089
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.00145
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.0016
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, wild-type enzyme
-
0.00174
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
0.00246
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.009
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
0.00047
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.00254
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme 0.00184 I192T/V306G
-
0.00303
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.00396
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
0.00398
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.00442
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.042
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
7
beta-D-galactose
mutant enzyme T41V, NADP+ as cofactor
8
beta-D-galactose
mutant enzyme T41V, NAD+ as cofactor
22
beta-D-galactose
mutant enzyme T41A, NADP+ as cofactor
37
beta-D-galactose
wild type enzyme, NADP+ as cofactor
56
beta-D-galactose
mutant enzyme T41A, NAD+ as cofactor
61
beta-D-galactose
wild type enzyme, NAD+ as cofactor
4
beta-D-glucose
mutant enzyme T41V, NADP+ as cofactor
6
beta-D-glucose
mutant enzyme T41V, NAD+ as cofactor
14
beta-D-glucose
mutant enzyme T41A, NADP+ as cofactor
18
beta-D-glucose
-
E96K mutant, coenzyme NADP+
19.34
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
23
beta-D-glucose
-
E96K mutant, coenzyme NAD+
39
beta-D-glucose
mutant enzyme T41A, NAD+ as cofactor
48
beta-D-glucose
wild type enzyme, NADP+ as cofactor
68.23
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
75
beta-D-glucose
wild type enzyme, NAD+ as cofactor
92
beta-D-glucose
-
E96G mutant, coenzyme NADP+
97
beta-D-glucose
-
E96A mutant, coenzyme NAD+
98
beta-D-glucose
-
E96A mutant, coenzyme NADP+
114
beta-D-glucose
-
E96G mutant, coenzyme NAD+
120
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH I
140
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH II
186
beta-D-glucose
-
Y253C mutant, coenzyme NADP+
190
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzymes GlcDH I and GlcDH II
200
beta-D-glucose
-
Y253C mutant, coenzyme NAD+
260
beta-D-glucose
-
wild type, coenzyme NADP+
300
beta-D-glucose
-
Q252L mutant, coenzyme NADP+
317
beta-D-glucose
-
mutant Q252L, pH 8.0, 25°C
334
beta-D-glucose
-
mutant Q252L/E170K, pH 8.0, 25°C
390
beta-D-glucose
-
wild type, coenzyme NAD+
395
beta-D-glucose
-
wild-type enzyme, pH 8.0, 25°C
420
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzyme GlcDH IV
430
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzyme GlcDH III
462
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP, isoenzyme GlcDH IV
802
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH III
11.1
D-glucose
-
coenzyme NAD+
14.7
D-glucose
-
coenzyme NADP+
19.34
D-glucose
cosubstrate NADP+, 70°C, pH not specified in the publication
41
D-glucose
-
coenzyme NADP+
45.9
D-glucose
-
coenzyme NAD+
68.23
D-glucose
cosubstrate NAD+, 70°C, pH not specified in the publication
70
D-glucose
-
at pH 8.0 and 37°C
81.9
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R
82.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
82.6
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P
84.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K
87.84
D-glucose
pH 8.0, 25°C
89.6
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R
112
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
119
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
190
D-glucose
isozyme GlcDH-I
190
D-glucose
isozyme GlcDH-II
317
D-glucose
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
334
D-glucose
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
352
D-glucose
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
390
D-glucose
isozyme GlcDH-IWG3
395
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
1.5
D-glucose 6-phosphate
-
-
1.5
D-glucose 6-phosphate
-
coenzyme NADP+
1.6
D-glucose 6-phosphate
-
coenzyme NAD+
12.7
D-glucose 6-phosphate
-
coenzyme NADP+
14.2
D-glucose 6-phosphate
-
coenzyme NAD+
7
D-xylose
mutant enzyme T41V, NADP+ as cofactor
12
D-xylose
mutant enzyme T41V, NAD+ as cofactor
22
D-xylose
mutant enzyme T41A, NADP+ as cofactor
44
D-xylose
wild type enzyme, NADP+ as cofactor
61
D-xylose
wild type enzyme, NAD+ as cofactor
81
D-xylose
mutant enzyme T41A, NAD+ as cofactor
0.00008
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00095
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00162
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
0.00283
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T
0.00286
NAD+
pH and temperature not specified in the publication, mutant enzyme I192V
0.00678
NAD+
pH and temperature not specified in the publication, wild-type enzyme
0.00838
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
54.47
NAD+
cosubstrate D-glucose, 65°C, pH not specified in the publication
61.3
NAD+
with beta-D-galactose, pH 7.5, 70°C
70.49
NAD+
cosubstrate D-glucose, 70°C, pH not specified in the publication
74.9
NAD+
with beta-D-glucose, pH 7.5, 70°C
105.4
NAD+
cosubstrate D-glucose, 80°C, pH not specified in the publication
115
NAD+
wild type enzyme, at pH 8.0 and 25°C
180
NAD+
mutant enzyme DS255, at pH 8.0 and 25°C
390
NAD+
-
wild type, coenzyme NAD+
521000
NAD+
-
at pH 8.0 and 25°C
18
NADP+
-
E96K mutant
26.74
NADP+
cosubstrate D-glucose, 65°C, pH not specified in the publication
28.52
NADP+
cosubstrate D-glucose, 70°C, pH not specified in the publication
37.4
NADP+
with beta-D-galactose, pH 7.5, 70°C
44.17
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
47.7
NADP+
with beta-D-glucose, pH 7.5, 70°C
93
NADP+
wild type enzyme, at pH 8.0 and 25°C
130
NADP+
mutant enzyme DS255, at pH 8.0 and 25°C
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E170K
-
decrease in melting temperature by 7.1 degrees
E170K/K252L
-
increase in melting temperature by 5.6 degrees
F155Y
-
increase in melting temperature by 1.9 degrees
K252L
-
increase in melting temperature by 8.9 degrees
K252Q
-
decrease in melting temperature by 2.7 degrees
A11L
-
slight decrease in half-life at 25°C, decrease in specific activity
A246V
-
slight decrease in half-life at 25°C, decrease in specific activity
E170K
-
increase in melting temperature by 25.9 degrees
E170R
-
increase in half-life at 65°C
F155Y
-
slight increase in half-life at 25°C, almost 100% increase in specific activity
G114E
-
slight increase in half-life at 25°C, decrease in specific activity
G28A
-
slight decrease in half-life at 25°C, decrease in specific activity
I12V
-
slight decrease in half-life at 25°C, 4fold decrease in specific activity
I186V
-
slight increase in half-life at 25°C, decrease in specific activity
I75M
-
slight decrease in half-life at 25°C, decrease in specific activity
I90V
-
half-life at 25°C similar to wild-type, decrease in specific activity
K107E
-
slight decrease in half-life at 25°C, decrease in specific activity
K204E
-
no catalytic activity
K234D
-
no catalytic activity
M23I
-
slight increase in half-life at 25°C, decrease in specific activity
M89L
-
slight decrease in half-life at 25°C, slight increase in specific activity
N46A
-
slight increase in half-life at 25°C, decrease in specific activity
P105S
-
slight increase in half-life at 25°C, decrease in specific activity
P45A
-
slight increase in half-life at 25°C, 40% increase in specific activity
P45A/F155Y/E170K/V227A/Q252L
-
strong increase in half-life at 65°C, about 50% increase in specific activity
P45A/F155Y/E170R/V227A/W230F/Q252L
-
strong increase in half-life at 65°C, about 40% increase in specific activity
P45A/F155Y/V227A
-
strong increase in half-life at 25°C, 50% increase in specific activity
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
-
strong increase in half-life at 65°C, about 50% increase in specific activity
P45A/N46E/F155Y/V227A
-
strong increase in half-life at 25°C, decrease in specific activity
P45A/N46E/F155Y/V227A/W230F
-
increase in half-life at 65°C
P45A/V227A
-
strong increase in half-life at 25°C, decrease in specific activity
Q252L
-
increase in melting temperature by 17.3 degrees
Q252L/E170K
-
strong increase in half-life at 65°C, about 50% increase in specific activity
Q252L/E170R
-
strong increase in half-life at 65°C, about 50% increase in specific activity
Q31G
-
no catalytic activity
Q43E
-
half-life at 25°C similar to wild-type, slight increase in specific activity
V140I
-
slight decrease in half-life at 25°C, decrease in specific activity
V227A
-
slight increase in half-life at 25°C
W230F
-
no catalytic acitivity
G28A
-
slight decrease in half-life at 25°C, decrease in specific activity
-
K204E
-
no catalytic activity
-
P105S
-
slight increase in half-life at 25°C, decrease in specific activity
-
Q252L
-
increase in melting temperature by 17.3 degrees
-
Q252L/E170K
-
strong increase in half-life at 65°C, about 50% increase in specific activity
-
E170K
-
increase in melting temperature by 18.5 degrees
F155Y
-
increase in melting temperature by 4.5 degrees
L252Q
-
decrease in melting temperature by 19.3 degrees
A258F
Km (D-glucose) increased at pH 6 compared to wild-type, decreased at pH 8 compared to wild-type. Mutant shows higher substrate specificity with D-xylose, D-mannose, D-galactose and D-glucosamine compared to wild-type. Mutant shows a markedly deteriorated thermostability
DELTAG261
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type.Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Mutant shows a markedly deteriorated thermostability
E170K
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
E96K
-
mutation increases thermostability by about 15°C at pH 6.5
E96K/D108N/P194Q/E210K
mutant enzyme has higher stability at 60°C and 97% remaining activity compared to the wild type enzyme
E96K/V112A/E133K/Y217H
mutant enzyme has higher stability at 60°C and 85% remaining activity compared to the wild type enzyme
E96K/V183I
mutant enzyme has higher stability at 60°C and 72% remaining activity compared to the wild type enzyme
G259A
Km (D-glucose) increased at pH 6 and pH 8 compared to wild-type. Specific activity of the G259A mutant is slightly lower, but is still comparable with wild-type BmGlcDH-IV. Thermostability comparable to wild-type
G259V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261A
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
Q252L/A258G
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/K137R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I/K137R
the mutant enzyme exhibits a 9.2fold increase in tolerance against 10% (v/v) 1-phenylethanol and is more stable than mutant enzyme Q252L/E170K (BmGDHM0) when exposed to hydrophobic and enzyme-inactivating compounds such as acetophenone, ethyl 2-oxo-4-phenylbutyrate, and ethyl (R)-2-hydroxy-4-phenylbutyrate
E170K
-
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
-
Q252L
-
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
-
Q252L/E170K
-
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
-
E96A
-
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
-
E96G
-
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
-
Q252L
-
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
-
Q252L/A258G
-
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
-
Q252L/E170K
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/K166R
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R/V72I
-
kinetic parameters of the mutant enzyme are determined
-
Y253C
-
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
-
I192T
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
I192T/V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 3fold lower than the kcat/Km-value of the wild-type enzyme
I192T/V306I
mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor
V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are slightly higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 2fold lower than the kcat/Km-value of the wild-type enzyme
V306I
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
DS255
the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme
DS255
-
the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme
-
E96A
-
mutation increases thermostability at pH 6.5
E96A
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
E96G
-
mutation increases thermostability at pH 6.5
E96G
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
Q252L
-
mutation increases thermostability at pH 6.5
Q252L
-
natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme
Q252L
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
Q252L
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
Q252L/E170K
-
site-directed mutagenesis of the mutant strain IWG3, the mutant is insensitive against NaCl concentration and pH value, slightly increased activity compared to the wild-type enzyme
Q252L/E170K
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
Q252L/E170K
kinetic parameters of the mutant enzyme are determined
Y253C
-
mutation increases thermostability at pH 6.5
Y253C
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
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