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Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.47
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]
IUBMB Comments
This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
showSynonyms
hexose-6-phosphate dehydrogenase, glcdh-i, glcdh-ii, ssgdh, glcdh-iwg3, bmglcdh-iv, lsgdh, bzgdh, hexose phosphate dehydrogenase, nad(p)-dependent glucose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkali-resistant glucose 1-dehydrogenase
beta-D-glucose:NAD(P)+ 1-oxidoreductase
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bzgdh
D-glucose dehydrogenase (NAD(P))
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EC 1.1.5.2
GDH
GDHB
general stress protein 74
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GlcDH
GlcDH-I
GlcDH-II
GlcDH-IWG3
glucose 1-dehydrogenase
glucose 1-dehydrogenase 3
glucose 1-dehydrogenase B
glucose dehydrogenase
GluDH
GSP74
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hexose phosphate dehydrogenase
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hexose-6-phosphate dehydrogenase
LsGDH
NAD(P)-dependent glucose 1-dehydrogenase
NAD(P)-dependent glucose-1-dehydrogenase
NAD-GDH
nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase
SSO3204
additional information
GDH
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GlcDH
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-
-
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hexose-6-phosphate dehydrogenase
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-
-
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nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase
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nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase
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additional information
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enzyme belongs to the family of short-chain dehydrogenases/reductases
additional information
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enzyme belongs to the family of short-chain dehydrogenases/reductases
additional information
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enzyme belongs to the family of short-chain dehydrogenases/reductases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
ordered bi bi mechanism, formation of ternary complexes, NADP+ adds first, NADPH formed dissociates last, for reverse reaction, NADPH adds first, NADP+ leaves last
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D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
ordered bi bi mechanism
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D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
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D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential ordered bi-bi mechanism
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D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential type ordered bibi mechnanism
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D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential ordered bi-bi mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:NAD(P)+ 1-oxidoreductase
This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+).
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CAS REGISTRY NUMBER
COMMENTARY
9028-53-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxy-D-glucose + NADP+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADPH + H+
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Substrates: 5% of the activity with D-glucose and NAD+
Products: -
Products: -
?
2-deoxy-beta-D-xylose + NAD+
2-deoxy-D-xylono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-deoxy-D-glucose 6-phosphate + NAD+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADH
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-D-glucose + NADP+
? + NADPH
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Substrates: 9% of the activity with D-glucose and NAD+
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
Substrates: the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
Products: -
Products: -
ir
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH
Substrates: 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+
Products: -
Products: -
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
Substrates: 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+
Products: -
Products: -
ir
beta-D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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Substrates: 26% activity compared to D-glucose
Products: -
Products: -
r
D-allose + NADP+
D-allono-1,5-lactone + NADPH
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Substrates: 13% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-altrose + NADP+
D-altrono-1,5-lactone + NADPH
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Substrates: 12% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-fructose + NAD(P)+
? + NAD(P)H
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Substrates: no activity with mutants Q252L and Q252L/E170K
Products: -
Products: -
?
D-fructose + NAD+
?
Substrates: weak substrate
Products: -
Products: -
?
D-fructose + NADP+
?
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Substrates: 0.03% activity compared to D-glucose
Products: -
Products: -
?
D-galactose 6-phosphate + NAD+
6-phospho-D-galactono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-galactose 6-phosphate + NADP+
6-phospho-D-galactono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucosamine + NAD(P)+
?
Substrates: low activity
Products: -
Products: -
?
D-glucosamine + NADP+
D-glucosamino-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-glucose + 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
Substrates: -
Products: -
Products: -
?
D-glucose + 1-benzyl-3-carbamoylpyridin-1-ium chloride
D-glucono-1,5-lactone + reduced 1-benzyl-3-carbamoylpyridin-1-ium chloride
Substrates: -
Products: -
Products: -
?
D-glucose + 1-phenethyl-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-phenethyl-1,4-dihydropyridine-3-carboxamide
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
Substrates: -
Products: -
Products: -
?
D-gulose + NAD+
D-gulono-1,5-lactone + NADH
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Substrates: 8% of the activity with D-glucose
Products: -
Products: -
?
D-gulose + NADP+
D-gulono-1,5-lactone + NADPH
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Substrates: 12% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-idose + NAD+
D-idono-1,5-lactone + NADH
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Substrates: 65% of the activity with D-glucose
Products: -
Products: -
?
D-idose + NADP+
D-idono-1,5-lactone + NADPH
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Substrates: 12% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-lactose + NAD+
D-lactono-1,5-lactone + NADH + H+
Substrates: relative activity: 4.2%
Products: -
Products: -
?
D-lactose + NADP+
?
-
Substrates: 3.0% activity compared to D-glucose
Products: -
Products: -
?
D-lyxose + NAD(P)+
?
Substrates: low activity
Products: -
Products: -
?
D-maltose + NADP+
?
-
Substrates: 1.03% activity compared to D-glucose
Products: -
Products: -
?
D-mannose + NADP+
?
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Substrates: 11.53% activity compared to D-glucose
Products: -
Products: -
?
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
-
Substrates: 4% of the activity with D-glucose and NADP+
Products: -
Products: -
?
D-xylose + NADP+
?
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Substrates: 12.89% activity compared to D-glucose
Products: -
Products: -
?
sucrose + NAD+
?
Substrates: relative activity: 6.3%
Products: -
Products: -
?
2-amino-2-deoxy-D-glucose + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 14% of the activity with D-glucose
Products: -
Products: -
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 26% of the activity with D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD(P)+
?
Substrates: low activity
Products: -
Products: -
?
2-deoxy-D-glucose + NAD(P)+
?
-
Substrates: low activity
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 113% of the activity with D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Bacillus sp. (in: firmicutes) BG 1722
-
Substrates: 113% of the activity with D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 108% of the activity with D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 114% of the activity with D-glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 112% relative activity
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Priestia megaterium M1286
-
Substrates: 112% relative activity
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 12% of the activity with glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: 12% of the activity with glucose
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 103% of the activity with D-glucose and NAD+
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. (in: firmicutes) BG 1722
-
Substrates: 103% of the activity with D-glucose and NAD+
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 25% of the activity with D-glucose and NAD+
Products: -
Products: -
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
Substrates: 66% of the activity with D-glucose
Products: -
Products: -
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: 66% of the activity with D-glucose
Products: -
Products: -
?
beta-D-galactose + NAD+
D-galactono-1,5-lactone + NADH
A0A068FPP9
Substrates: 6.8% of the activity as compared to D-glucose
Products: -
Products: -
?
beta-D-galactose + NAD+
D-galactono-1,5-lactone + NADH
A0A068FPP9
Substrates: 6.8% of the activity as compared to D-glucose
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
Substrates: -
Products: -
Products: -
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: enzyme plays a role in germination
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: enzyme plays a role in germination
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
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?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: best substrate, wild-type and mutant enzymes
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beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: first step of the non-phosphorylative Entner-Doudoroff pathway
Products: -
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ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
Products: -
Products: -
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
Products: -
Products: -
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Corynebacterium sp. 150-1
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
Products: -
Products: -
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
Products: -
Products: -
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: about 3times more active with NADP+ than with NAD+
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: about 3times more active with NADP+ than with NAD+
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
Products: -
Products: -
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beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: the enzyme is highly specific for beta-D-glucose
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 9% of the activity with NAD+
Products: -
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beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: 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+
Products: -
Products: -
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beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 93% of the activity with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. (in: firmicutes) BG 1722
-
Substrates: 93% of the activity with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 1% of the activity with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Corynebacterium sp. 150-1
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 1% of the activity with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: in the reverse reaction only 4% of the reaction occurs at neutral pH
Products: -
Products: -
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: the enzyme is specific for NADP+ and completely inactive with NAD+
Products: -
Products: -
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: about 3times more active with NADP+ than with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: about 3times more active with NADP+ than with NAD+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: the enzyme is highly specific for beta-D-glucose
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 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+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 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+
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 100fold higher affinity for NADP+ than for NAD+
Products: -
Products: -
ir
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
Substrates: -
Products: -
Products: -
?
cellobiose + NAD+
? + NADH
-
Substrates: 89% of the activity with D-glucose
Products: -
Products: -
?
cellobiose + NAD+
? + NADH
-
Substrates: as active as glucose
Products: -
Products: -
?
cellobiose + NAD+
? + NADH
Corynebacterium sp. 150-1
-
Substrates: as active as glucose
Products: -
Products: -
?
cellobiose + NAD+
? + NADH
-
Substrates: as active as glucose
Products: -
Products: -
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
-
Substrates: 8% of the activity with D-glucose
Products: -
Products: -
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: 8% of the activity with D-glucose
Products: -
Products: -
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
-
Substrates: 5% of the activity with D-glucose
Products: -
Products: -
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: 5% of the activity with D-glucose
Products: -
Products: -
?
D-fructose + NAD+
? + NADH
-
Substrates: 9% of the activity with D-glucose
Products: -
Products: -
?
D-fructose + NAD+
? + NADH
-
Substrates: 9% of the activity with D-glucose
Products: -
Products: -
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
Substrates: -
Products: -
Products: -
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
Substrates: low activity with wild-type and mutant enzymes
Products: -
Products: -
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
Substrates: equally active compared to beta-D-glucose
Products: -
Products: -
?
D-galactose + NAD+
?
Substrates: weak substrate
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: 15% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
Saccharolobus solfataricus MT-4 / DSM 5833
-
Substrates: 15% of the activity with D-glucose and NAD+
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
Substrates: relative activity: 17.3%
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
Substrates: relative activity: 17.3%
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 9.1% (reference: D-glucose 100%)
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 2.9% (reference: D-glucose 100%)
Products: -
Products: -
?
D-galactose + NADP+
?
-
Substrates: 1.09% activity compared to D-glucose
Products: -
Products: -
?
D-galactose + NADP+
?
-
Substrates: 1.09% activity compared to D-glucose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: 5% of the activity with D-glucose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
Substrates: activity with substrate D-galactose in presence of cosubstrate NADP+
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
Substrates: activity with substrate D-galactose in presence of cosubstrate NADP+
Products: -
Products: -
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 11% (reference: D-glucose 100%)
Products: -
Products: -
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 3% (reference: D-glucose 100%)
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
Priestia megaterium IWG3
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
Priestia megaterium MI286
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Priestia megaterium IWG3
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
A0A068FPP9
Substrates: the enzyme prefers NAD+ rather than NADP+
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
A0A068FPP9
Substrates: the enzyme prefers NAD+ rather than NADP+
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: about 20% activity with D-galactose, D-xylose, maltose
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: relative activity: 100%
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: about 20% activity with D-galactose, D-xylose, maltose
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: relative activity: 100%
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: 100% relative activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium IAM 1030
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium IGW3
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium IWG3
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium IWG3
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium M1286
-
Substrates: 100% relative activity
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
A0A068FPP9
Substrates: the enzyme prefers NAD+ rather than NADP+
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
A0A068FPP9
Substrates: the enzyme prefers NAD+ rather than NADP+
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 100% activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: 75% relative activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Priestia megaterium M1286
-
Substrates: 75% relative activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: other substrates: hexose-6-phosphates, glucose-6-sulfate, glucose
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-maltose + NAD(P)+
? + NAD(P)H
-
Substrates: no activity with mutants Q252L and Q252L/E170K
Products: -
Products: -
?
D-maltose + NAD+
?
A0A068FPP9
Substrates: 10% of the activity as compared to D-glucose
Products: -
Products: -
?
D-maltose + NAD+
?
A0A068FPP9
Substrates: 10% of the activity as compared to D-glucose
Products: -
Products: -
?
D-maltose + NAD+
?
Substrates: relative activity: 22.4%
Products: -
Products: -
?
D-mannose + NAD(P)+
? + NAD(P)H
-
Substrates: wild-type and mutant enzymes
Products: -
Products: -
?
D-mannose + NAD+
?
Substrates: weak substrate
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
Substrates: 2% relative activity
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
Priestia megaterium M1286
-
Substrates: 2% relative activity
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
Substrates: relative activity: 7.6%
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
Substrates: relative activity: 7.6%
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 18% (reference: D-glucose 100%)
Products: -
Products: -
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 4.8% (reference: D-glucose 100%)
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: 88% of the activity with D-glucose
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: no activity
Products: -
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?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
Substrates: wild-type and mutant enzymes
Products: -
Products: -
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: 44% of the activity with D-glucose
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: 47% of the activity with D-glucose
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Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Corynebacterium sp. 150-1
-
Substrates: 47% of the activity with D-glucose
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: 47% of the activity with D-glucose
Products: -
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: 44% of the activity with D-glucose
Products: -
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Substrates: relative activity: 22.5%
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 35% (reference: D-glucose 100%)
Products: -
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Substrates: substrate specificity wild-tpye: 10% (reference: D-glucose 100%)
Products: -
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?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: 28% of the activity with D-glucose and NAD+
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
A0A068FPP9
Substrates: 6.1% of the activity as compared to D-glucose
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
A0A068FPP9
Substrates: 6.1% of the activity as compared to D-glucose
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: 28% of the activity with D-glucose and NAD+
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: activity with substrate D-galactose in presence of cosubstrate NADP+
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: activity with substrate D-galactose in presence of cosubstrate NADP+
Products: -
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?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
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?
gentiobiose + NAD+
? + NADH
-
Substrates: 103% of the activity with gentiobiose
Products: -
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?
gentiobiose + NAD+
? + NADH
-
Substrates: 86% of the activity with D-glucose
Products: -
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?
gentiobiose + NAD+
? + NADH
Corynebacterium sp. 150-1
-
Substrates: 103% of the activity with gentiobiose
Products: -
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?
gentiobiose + NAD+
? + NADH
-
Substrates: 103% of the activity with gentiobiose
Products: -
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?
gluconate + NAD+
? + NADH
-
Substrates: -
Products: -
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?
maltose + NAD+
? + NADH
-
Substrates: 6% of the activity with D-glucose
Products: -
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?
maltose + NAD+
? + NADH
Bacillus sp. (in: firmicutes) BG 1722
-
Substrates: 6% of the activity with D-glucose
Products: -
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?
maltose + NADP+
? + NADPH
-
Substrates: 5% of the activity D-glucose and NAD+
Products: -
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?
maltose + NADP+
? + NADPH
Bacillus sp. (in: firmicutes) BG 1722
-
Substrates: 5% of the activity D-glucose and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with sucrose
Products: -
Products: -
?
additional information
?
-
Substrates: Cys residues are not involved in the catalytic site
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity of wild-type and mutant enzymes with sucrose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
Products: -
Products: -
?
additional information
?
-
Priestia megaterium M1286
-
Substrates: no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
Products: -
Products: -
?
additional information
?
-
Substrates: D-ribose, maltose, lactose and sucrose are poor substrates, no activity with D-allose, D-arabinose, and D-mannose
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, no activity with D-mannose, D-ribose, and glucose 6-phosphate, cofactor specificity depends on the sugar sustrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
Substrates: the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
Products: -
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ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 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+
Products: -
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?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: enzyme plays a role in germination
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: enzyme plays a role in germination
Products: -
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?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: first step of the non-phosphorylative Entner-Doudoroff pathway
Products: -
Products: -
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
Priestia megaterium IWG3
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the catalytic alpha-subunit contains a FAD binding motif at the N-terminal region
additional information
dual cofactor specificity due to presence of Asn215, His217, and the GXGXXA motif
-
NAD+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
NAD+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
NAD+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
NAD+
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+
NAD+
kcat/Km of glucose in reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+
NADP+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
NADP+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
NADP+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
NADP+
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+
NADP+
kcat/Km of glucose in reaction with NADP+ is about 8fold higher compared to kcat/Km of glucose in the reaction with NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(NH4)2SO4
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
K+
KCl
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
Li+
Mg2+
Mn2+
Na+
Na2SO4
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
NaCl
NH4+
Zn2+
additional information
NaCl
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
Zn2+
enzyme contains the catalytic zinc binding residues Cys39 and His66, no increase in activity by addition of 0.1 mM ZnCl2
additional information
enzyme does not contain weakly associated metal ions
additional information
not affected by 0.1 mM CaCl2 and MgCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, room temperature, pH 9.0, rapid inactivation
3-(2-bromoacetyl)pyridine
active-site-directed irreverseible inhibitor, the cofactor NAD but not the substrate glucose protects the enzyme from the inactivation, in the presence of 0.1 M NAD and 1.37 mM 3-(2-bromoacetyl)pyridine, glucose dehydrogenase has still 85% of its original activity after incubation for 2 h
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, room temperature, pH 9.0, 50% inactivation
D-glucono-1,5-lactone
-
forward reaction, oxidation, product inhibition, noncompetitive vs. beta-D-glucose and NADP+
N-ethylmaleimide
-
3 mM, room temperature, pH 9.0, 50% inactivation
Tetranitromethane
the rapid inactivation can be prevented by the presence of NAD, AMP, or ATP
Ca2+
60% inhibition at 50, 100 and 10 mM in sodium phosphate buffer at pH 8.0, Tris/HCl buffer at pH 8.0 and Tris/HCl buffer at pH 9.0, respectively
NaCl
-
reaction rate and dissociation at pH 9 are reduced by increasing the NaCl concentration (0-500 mM)
NADP+
-
reverse reaction, reduction, product inhibition, competitive vs. NADPH and noncompetitive vs. D-glucono-1-5-lactone
additional information
no inhibition by EDTA and thiol reagents such as fluorescein 5-maleimide
-
additional information
-
hexadecyltrimethylammonium bromide, i.e. CTAB, does not influence the enzyme activity but increases the enzyme stability
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
AMP
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
ATP
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
dipicolinic acid
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
NAD+
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
NADH
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
NADPH
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
additional information
-
hexadecyltrimethylammonium bromide, i.e. CTAB, does not influence the enzyme activity but increases the enzyme stability
-
NADP+
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
NADP+
-
2 mM NADP+ transforms enzyme at 70°C within 10 min from inactive to active state
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.17
D-glucose
cosubstrate NADP+, 70°C, pH not specified in the publication
4.59
D-glucose
cosubstrate NAD+, 70°C, pH not specified in the publication
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
14
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 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
17.5
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
0.0015
D-glucose 6-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.049
D-glucose 6-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.15
NAD+
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
0.17
NAD+
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°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
0.33
NAD+
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 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
0.86
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
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
0.026
NADP+
-
pH not specified in the publication, temperature not specified in the publication
0.14
NADP+
cosubstrate D-glucose, 70°C, pH not specified in the publication
0.15
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
0.15
NADP+
cosubstrate D-glucose, 65°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
190
beta-D-glucose
-
pH 8.0, 30°C, coenzyme NAD+, isoenzymes GlcDH I and GlcDH II
19.34
D-glucose
cosubstrate NADP+, 70°C, pH not specified in the publication
68.23
D-glucose
cosubstrate NAD+, 70°C, pH not specified in the publication
82.4
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
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
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
395
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
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
70.49
NAD+
cosubstrate D-glucose, 70°C, pH not specified in the publication
105.4
NAD+
cosubstrate D-glucose, 80°C, pH not specified in the publication
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
44.17
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
0.00006
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
0.00009
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
0.00011
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
0.00018
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
0.00073
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.0017
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00006
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T
0.00009
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306G
0.00011
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306I
0.00016
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, wild-type enzyme
0.00019
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192V
0.00104
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00164
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00004
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
0.0002
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
0.00024
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
0.00029
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
0.00058
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00063
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
0.00517
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
4.7
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
6.5
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
6.9
D-glucose
pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
14.86
D-glucose
cosubstrate NAD+, 70°C, pH not specified in the publication
115.2
D-glucose
cosubstrate NADP+, 70°C, pH not specified in the publication
0.00019
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00061
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
0.000974
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
0.00565
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00613
NAD+
pH and temperature not specified in the publication, mutant enzyme I192V
0.00778
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T
0.01594
NAD+
pH and temperature not specified in the publication, wild-type enzyme
9.74
NAD+
cosubstrate D-glucose, 65°C, pH not specified in the publication
31.6
NAD+
cosubstrate D-glucose, 70°C, pH not specified in the publication
31.95
NAD+
cosubstrate D-glucose, 80°C, pH not specified in the publication
178.3
NADP+
cosubstrate D-glucose, 65°C, pH not specified in the publication
203.7
NADP+
cosubstrate D-glucose, 70°C, pH not specified in the publication
294.5
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.18
0.284
-
NAD-GDH, using 10g/l gluconate as excessive carbon source and 0.132 g/l (NH4)SO4
0.31
0.34
-
NAD-GDH, using 10 g/l glucose as limited carbon source and 1.32 g/l (NH4)SO4
0.36
-
beta-D-glucose as substrate and a mixture of beta-D-glucose, L-arabinose, D-xylose, D-galactose, D-maltose, D-mannose and D-cellobiose as carbon source (15 mmol/l each)
0.38
-
beta-D-glucose as the sole carbon source and a mixture of beta-D-glucose, L-arabinose, D-xylose, D-galactose, D-maltose, D-mannose and D-cellobiose as substrate (15 mmol/l each)
0.4
-
NAD-GDH, using 10 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.55
-
beta-D-glucose as the sole carbon source and L-arabinose as substrate
0.6
-
beta-D-glucose as the sole carbon source and D-mannose as substrate
0.62
-
beta-D-glucose as the sole carbon source and D-maltose as substrate
0.67
-
NAD-GDH, using 50 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.72
-
NAD-GDH, using 20 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.78
-
beta-D-glucose as the sole carbon source and D-xylose as substrate
0.83
-
beta-D-glucose as the sole carbon source and beta-D-glucose as substrate
0.91
-
beta-D-glucose as the sole carbon source and D-galactose as substrate
1.1
-
NAD-GDH, using 30 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
167
169
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R
172
227
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I
239
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R
additional information
0.18
-
NAD-GDH, using 10g/l gluconate as excessive carbon source and 1.32 g/l (NH4)SO4
0.31
-
beta-D-glucose as the sole carbon source and D-cellobiose as substrate
167
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P
167
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R
172
substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
6.5
7.5
8.5 - 9
9.5
9.8
8.5 - 9
-
higher reaction rate in Tris-HCl buffer compared to potassium phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
when incubated for 6 h at 37°C, the enzyme is highly stable in acidic conditions (pH 5.0-6.0) but is completely inactivated at pH values above 8.0
5.5 - 10.5
-
the enzyme's activity is more than 60% of its maximum at pH values ranging from 5.5 to 10.5
6 - 9.5
-
pH 6.0: about 40% of maximal activity, pH 9.5: about 45% of maximal activity
7 - 10
7 - 8.5
-
pH 7.0: 70% of maximal activity with glucose and NAD+ and about 55% of the activity with glucose and NADP+, pH 8.5: about 55% of maximal activity with glucose and NAD+ and about 75% of the activity with glucose and NADP+
7.5 - 10.5
-
at pH 7.5 and 10.0 respectively 75% and 50% activity compared to optimal pH
8.5 - 12
-
pH 8.5: about 35% of maximal activity, pH 12.0: about 65% of maximal activity
additional information
-
sharp drop in activity at alkaline pH of wild-type and mutant Q252L activities, not mutant Q252L/E170K
7 - 10
A0A068FPP9
pH 7.0: about 40% of maximal activity, pH 10.0: about 45% of maximal activity
7 - 10
-
more than 60% activity between pH 7.0 and 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
45
50
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20°C: about 70% of maximal activity, 40°C: about 60% of maximal activity
25 - 55
A0A068FPP9
25°C: about 60% of maximal activity, 55°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 4.8
4.7 - 4.8
-
isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed
6
-
isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Priestia megaterium IAM 1030
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase
brenda
-
nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase
-
brenda
-
enzyme resides on the luminal side of liver microsomes
brenda
-
enzyme resides on the luminal side of liver microsomes
brenda
-
pyrrolo-quinoline-quinone-linked glucose dehydrogenase
-
brenda
-
pyrrolo-quinoline-quinone-linked glucose dehydrogenase
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
identification (single-nucleotide polymorphism) of hexose-6-phosphate dehydrogenase as a risk gene for multiple sclerosis
physiological function
physiological function
-
plays a role in maintaining normal NADPH levels and redox environment inside the endoplasmic reticulum
physiological function
the enzyme is involved in glucose catabolism via the branched EntnerDoudoroff pathway
Show AA Sequence and Transmembrane Helices (1958 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
160000
230000
27800
28000
28200
29000
30000
38000
40000
41000
84000
-
in the presence of 1 mM NADP+, without NADP+ enzyme forms aggregates, gel filtration
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
tetramer
additional information
homodimer
-
2 * 28048, calculated from amino acid sequence
homodimer
-
2 * 28048, calculated from amino acid sequence
-
homotetramer
4 * 28000, SDS-PAGE, 120000 kDa by gel filtration, calculated: 261 amino acid residues, 27.8 kDa
homotetramer
-
4 * 28000, SDS-PAGE, 120000 kDa by gel filtration, calculated: 261 amino acid residues, 27.8 kDa
-
homotetramer
a significant hydrogen bond network is formed between the residue R166 of subunit A and E148 of both subunits A and B in mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R. In the homotetramer structure of wild-type enzyme BmGDH, the same interactions occur between subunit C (R166) and subunit D (E148)
homotetramer
Priestia megaterium IWG3
-
a significant hydrogen bond network is formed between the residue R166 of subunit A and E148 of both subunits A and B in mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R. In the homotetramer structure of wild-type enzyme BmGDH, the same interactions occur between subunit C (R166) and subunit D (E148)
-
tetramer
-
2 * 45000, gel filtration of inactive monomeric enzyme
tetramer
Bacillus sp. (in: firmicutes) BG 1722
-
2 * 45000, gel filtration of inactive monomeric enzyme
-
additional information
-
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers
additional information
-
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers
additional information
-
at very low ionic strength, the tetrameric state becomes unstable, even at pH 6.5
additional information
-
monomers, dimers and tetramers participate in aggregation equilibria which are dependent on enzyme and NaCl concentration and on the pH value
additional information
-
complete dissociation at pH 9 is possible only at NaCl and KH2PO4 concentrations below 20 mM
additional information
-
reversible dissociation in to inactive monomers at alkaline pH
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
the lipid component may be involved in the molecular structure and function of the enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
precipitate collected by centrifugation and dissolved in a minimal volume of 0.1 M potassium phosphate buffer, pH 7.5, 1 mM 2-mercaptoethanol
-
1.7 A resoluton, four subunits are interrelated by three mutually perpendicular diad axes P,Q and R
batch method using ammonium sulfate as precipitant at pH 6.5 and microdialysis technique with 60% ammonium sulfate in 334 mM NAD, pH 5.8-6.8
-
hanging drop vapour diffusion method with 28% (w/v) PEG 2000, 4 mM NAD+, 40 mM sodium phosphate pH 6.0
the crystal structures of BmGlcDH-IV in ligand-free, NADH-bound and beta-D-glucose-bound forms is determined to a resolution of 2.0 A
hanging-drop vapour diffusion using a mother liquor of 12% (v/v) polyethylene glycol 4000, 0.1 M MES (pH 5.8), and 3% (v/v) propan-2-ol
precipitate is dissolved in deionized water and ammonium sulfate added to 23% saturation
-
2.9 A resolution, monomer comprises a central nucleotide-binding domain
-
hanging-drop vapour diffusion, 2% polyethylene glycol, pH 5.3, 0.4 mM NADP+, 3.0 A resolution, space group P6122
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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/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
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
A11L
-
slight decrease 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
-
I75M
-
slight decrease in half-life at 25°C, decrease in specific activity
-
V140I
-
slight decrease in half-life at 25°C, decrease in specific activity
-
DS255
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
E96A
E96G
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
Q252L/A258G
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K
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
Y253C
E170K
Priestia megaterium IGW3
-
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
-
Q252L
Priestia megaterium IGW3
-
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
-
Q252L/E170K
Priestia megaterium IGW3
-
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
-
E96A
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
-
E96G
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
-
E96K/V183I
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 72% remaining activity compared to the wild type enzyme
-
Q252L
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
-
Q252L/A258G
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
-
Q252L/E170K/K166R
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R/V72I
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
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
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
-
natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme
Q252L
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
Q252L
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
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
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
-
after 30 min at pH 3.0-11.0, the enzyme maintains activity of more than 70%
4 - 10
-
30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity
4 - 10.5
-
the enzyme is extremely stable over a broad pH ranges from 4.0 to 10.5 and retains more than 80% of its original activity after incubation at pH values ranging from 4.5 to 10.5
4 - 8.5
A0A068FPP9
1 h incubation, the enzyme maintains around 80% of its initial activity
5
-
30°C, 20 min, about 55% loss of activity of mutant enzyme Y253C, about 35% loss of activity of mutant enzyme E96G and wild-type enzyme
6.5 - 10.5
most stable at pH 8.5, retains more than 80% activity at pH 6.5-10.5 after 1 h at 25°C, more than 30% activity after 24 h at pH 10.0
6.5 - 7
-
20 min, without NaCl, isoenzyme GlcDH-IWG3 and GlcDH-III are stable
6.5 - 9
-
the enzyme is stable and active at pH 6.5, by shifting the pH to 9.0 the enzyme is completely and irreversibly dissociated into four inactive protomers
7 - 9
wild type GlcDH shows reversible dissociation-association between inactive monomers and active tetramers when the pH is shifted between 9 and 7
additional information
8
-
30°C, 20 min, about 50% loss of activity of mutant enzyme Y253C, about 80% loss of wild-type enzyme, about 30% loss of activity of mutant enzyme E96G and E96, about 15% loss of activity of mutant enzyme E96K
9
-
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9 the enzyme is completely and reversibly dissociated into four inactive protomers
9
after dissociation of the tetrameric enzyme into its inactive monomers at pH 9 two tyrosine residues (Tyr-254 and Tyr-160) become susceptible to nitration which are unable to reassociate to the tetramer
additional information
-
shifting the pH from 6.5 to 9.0 leads to inactivation, reactivation to 100% activity by shifting pH back to 6.5, protein concentration higher than 0.1 mg/ml
additional information
-
isoenzyme GlcDHIII has no stable pH-region without NaCl
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 35
stable for 1 week at 30°C (pH 6.5), completely inactivated in 30 min at 55°C, limited protection by glycerol, 84% activity after 30 min at 65°C in the presence of 2 M NaCl,
25 - 80
-
the enzyme shows considerable thermal stability after incubation for 30 min at temperature ranging from 25 to 80°C and maintains 20% of its maximum activity at 70°C
30
-
20 min, isoenzyme GlcDH-III, without NaCl, about 55% loss of activity
30 - 65
-
after 30 min at 30-65°C, the enzyme maintains high activity of more than 85%
40
45
50
55
60
65
70
-
20 min, presence of 2 mM NaCl, complete inactivation of isoenzyme GlcDH-III and GlcDH-IV, isoenzyme GlcDH-IWG3 loses 30% of initial activity
additional information
45
-
20 min, isoenzyme GlcDH-IV, without NaCl, about 35% loss of activity, isoenzyme IWG3, without NaCl, about 10% loss of activity
50
-
20 min, isoenzyme GlcDH-IWG3, without NaCl, complete loss of activity, isoenzymes GlcDH-II and GlcDH-IWG3 are stable in presence of 2 M NaCl
50
-
pH 6.5, 20 min, complete inactivation of wild-type enzyme, mutant enzyme E96K, E96G, E96A, Q252L and Y253C are stable
50
GlcDH-I1 is the most resistant isozyme against heat inactivation at 50°C (pH 6.5)
55
-
90% activity lost after 5 h in soluble native enzyme and GlcDHCys44 mutant enzyme, immobilized GlcDHCys44 mutant enyzyme loses 20% activity
55
-
pH 6.5, 20 min, about 65% loss of acticity of mutant enzyme Y253C, about 20% loss of activity of mutant enzyme Y252L, mutant enzyme E96K, E96G and E96A are stable
60
the enzyme shows half-lives of 23100, 364.5, and 5.3 min after 10 min at 30°C, 40°C, and 50°C, respectively. The enzyme is inactive after 10 min at 60°C
60
-
pH 6.5, 20 min, complete loss of activity of enzyme Y253C about 95% loss of activity of mutant enzyme Y252L, about 30% loss of activity of mutant enzyme E96G, mutant enzymes E96K and E95A are stable
65
-
half-life of wild-type, 8.7 min, of mutant K252L, 7.1 min, of mutant E170L/K252L, 4.2 min
65
-
half-life of wild-type, below 0.05 min, of mutant E170K 8.7 min, of mutant Q252L, 0.5 min, of mutant E170K/Q252L, 5323 min
65
-
20 min, in presence of 2 M NaCl, isoenzyme GlcDH-III loses about 30% of initial activity, isoenzyme GlcDH-IV loses about 10% of initial activity, isoenzyme IWG2 is stable
65
-
pH 6.5, 20 min, complete loss of activity of mutant enzyme Q252L, about 50% loss of activity of mutant enzyme E96K, about 10% loss of activity of mutant enzyme E96A
additional information
-
thermostability is highly increased by addition of NaCl
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2 M urea, 24 h, room temperature, no loss of activity, slow decrease at 4 M
-
enzyme shows good stability at low water content and at low salt concentration in reverse micelles
-
glucose dehydrogenase isoenzymes are stabilized in presence of 2 M NaCl. The effect is especially large for GlcDH-III, which is the most unstable enzyme
-
purified enzyme is indefinitely stable in the frozen state or in solution at pH 6.5 containing 3 M NaCl and a protein concentration of more than 0.5 mg/ml. Diluted enzyme solutions can be stabilized to the same degree by adding 0.5% polyvinylpyrrolidone. Any reduction of the ionic strength of enzyme solution leads to an irreversible inactivation which can be only partially prevented by additrion of polyvinylpyrrolidone
-
unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl
-
unstable at low ionic strength, in 67 mM phosphate buffer enzyme activity decreases to 80% within 5 hours at pH 6.5 and 0.01 mg/ml protein, reduction to 57% at 40 mM phosphate, high concentration of NAD inhibit dissociation
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-hexanol
1-phenylethanol
2-hexanol
Acetone
acetophenone
cyclohexane
-
enzyme is solubilized in reverse micelles of hexadecyltrimethylammonium bromide in cyclohexane with n-butanol as cosurfactant and retaines activity and catalytic properties in the organic medium
DMSO
Ethanol
isopropanol
Methanol
n-Butanol
-
enzyme is solubilized in reverse micelles of hexadecyltrimethylammonium bromide in cyclohexane with n-butanol as cosurfactant and retaines activity and catalytic properties in the organic medium
n-hexane
n-hexanol
n-propanol
1-hexanol
-
the enzyme exhibits an extreme tolerance towards 1-hexanol with 6%loss of activity at 10% (v/v)
1-hexanol
-
the enzyme exhibits an extreme tolerance towards 1-hexanol with 6%loss of activity at 10% (v/v)
-
1-phenylethanol
mutant enzymes Q252L/E170K/S100P and Q252L/E170K/K166R display a 2.9fold and 2.0fold improvement in tolerance against 1-phenylethanol, respectively, compared with mutant enzyme Q252L/E170K. The half-life (t1/2) of mutant enzyme Q252L/E170K/S100P/K166R in the presence of 10% (v/v) 1-phenylethanol is prolonged from 70.4 min to 319 min, representing a 4.5fold increase compared with mutant enzyme Q252L/E170K. The chemical tolerance of mutant enzyme Q252L/E170K/S100P/K166R/V72I and mutant enzyme Q252L/E170K/S100P/K166R/K137R against 10% (v/v) 1-phenylethanol is increased by 5.6fold and 6.7fold, respectively, compared with mutant enzyme Q252L/E170K
1-phenylethanol
Priestia megaterium IWG3
-
mutant enzymes Q252L/E170K/S100P and Q252L/E170K/K166R display a 2.9fold and 2.0fold improvement in tolerance against 1-phenylethanol, respectively, compared with mutant enzyme Q252L/E170K. The half-life (t1/2) of mutant enzyme Q252L/E170K/S100P/K166R in the presence of 10% (v/v) 1-phenylethanol is prolonged from 70.4 min to 319 min, representing a 4.5fold increase compared with mutant enzyme Q252L/E170K. The chemical tolerance of mutant enzyme Q252L/E170K/S100P/K166R/V72I and mutant enzyme Q252L/E170K/S100P/K166R/K137R against 10% (v/v) 1-phenylethanol is increased by 5.6fold and 6.7fold, respectively, compared with mutant enzyme Q252L/E170K
-
2-hexanol
-
the enzyme exhibits an extreme tolerance towards 2-hexanol with 7%loss of activity at 50% (v/v)
2-hexanol
-
the enzyme exhibits an extreme tolerance towards 2-hexanol with 7%loss of activity at 50% (v/v)
-
Acetone
Saccharolobus solfataricus MT-4 / DSM 5833
-
50%, 24 h, room temperature, no loss of activity
-
acetophenone
mutant enzyme Q252L/E170K retains 8% of initial activity when incubated for 12 h with 10% acetophenone
acetophenone
Priestia megaterium IWG3
-
mutant enzyme Q252L/E170K retains 8% of initial activity when incubated for 12 h with 10% acetophenone
-
DMSO
-
the enzyme exhibits an extreme tolerance towards DMSO with 1% loss of activity at 50% (v/v)
DMSO
-
the enzyme exhibits an extreme tolerance towards DMSO with 1% loss of activity at 50% (v/v)
-
DMSO
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) DMSO
DMSO
Priestia megaterium IWG3
-
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) DMSO
-
isopropanol
enzyme exhibits high tolerance to 30% isopropanol
Methanol
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) metanol
Methanol
Priestia megaterium IWG3
-
mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) metanol
-
Methanol
Saccharolobus solfataricus MT-4 / DSM 5833
-
50%, 24 h, room temperature, no loss of activity
-
n-hexane
-
the enzyme exhibits an extreme tolerance towards n-hexane with no loss of activity at 50% (v/v)
n-hexane
-
the enzyme exhibits an extreme tolerance towards n-hexane with no loss of activity at 50% (v/v)
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM phosphate buffer, pH 7.3, 1 mM 2-mercaptoethanol, 50% v/v glycerol, stable for at least 3 months
-
-20°C, 25 mM sodium phosphate buffer (pH 6.5) with 20% glycerol (w/v), 1 year, no loss of activity
-80°C, in CPB buffer (pH 6.0), at least 4 months, no loss of activity
-
4°C, 89% loss of activity after 4 days without stabilzing agent, complete stabilization by 10 mM NAD+ or 10 mM NADP+, and to a lesser extent by 800 mM NaCl. Partial stabilization by 800 MM (NH4)2SO4, 800 mM Na2SO4 or 800 mM dipicolinic acid
-
5°C, crystalline preparation as suspension in ammonium sulfate, stable for 6 months
-
5°C, crystalline preparation, in ammonium sulfate suspension, stable for several months
-
room temperature, 100 mM phosphate buffer at pH 7.0, 1 week, 30% loss of activity
-
room temperature, 100 mM phosphate buffer at pH 7.0, 3 days, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
80°C, anion-exchange chromatography, hydrophobic chromatography, gel filtration with 1 mM NADP+
-
ammonium sulfate, Sepharose 6B, DEAE-Sepharose, hydroxyapatite chromatography
-
DEAE-cellulose, partially purified enzyme, 10 mM NAD(P)+ protects from inactivation on column
-
DEAE-Sephadex, Blue-Dextran Sepharose, DEAE-Sephadex, crystallization
-
DEAE-Sepharose, 2',5'-ADP-Sepharose, Sephacryl
expressed in Escherichia coli, introduced cystein residue at position 44, ammonium sulfate, phenyl-Sepharose, thiopropyl-Sepharose
-
gel filtration on Superdex 75 26/60, anion exchange chromatography, and affinity chromatography using Reactive Red-500 dye affinity medium and an NaCl gradient of 0 to 1.5 M
gel filtration, DEAE-cellulose, hydroxylapatite, omega-aminohexyl-agarose
-
methanol extraction, Mono Q, Matrex Gel Red A, Mono P, gel filtration
-
native enzyme by gel filtration, recombinant enzyme from Escherichia coli by heat denaturation, and affinity gel chromatography
recombinant enzyme from Escherichia coli
recombinant enzyme from Escherichia coli by heat treament and 2 chromatographical steps
-
recombinant enzyme is solubilized in reverse micelles of hexadecyltrimethylammonium bromide, i.e. CTAB, in cyclohexane with n-butanol as cosurfactant
-
streptomycin treatment, ammonium sulfate, DEAE-cellulose, gel filtration, DE 52 cellulose, hydroxyl apatite, gel filtration
-
Triton X-100, acid treatment, ammonium sulfate, Sephacryl S-200, Sephacryl S-300, DEAE-cellulose, Sephacryl S-300
-
Triton X-114, acid treatment, ammonium sulfate, Sephacryl S-200, Sephacryl S-300, SE-cellulose, DEAE-cellulose, purified enzyme contains 1.7% lipid
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of the catalytic alpha-subunit in Escherichia coli as active water-soluble protein
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli
DNA sequence determination and analysis, expression in Escherichia coli strain JM109
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain JM109
expression in Escherichia coli
expression in Escherichia coli BL21(DE3) with a combined lac and T7 promoter
-
gene ST1704, expression in enzyme-deficient Escherichia coli strain
-
heterogeneously expressed in Escherichia coli BL21 (DE3)
A0A068FPP9
overexpression in Escherichia coli, short-chain dehydrogenase/reductase from Thermus thermophilus HB8 and the glucose dehydrogenase from Thermoplasma acidophilum DSM 1728 are simultaneously over-expressed by heterologous expression with pETDuet
-
DNA sequence determination and analysis, expression in Escherichia coli strain JM109
-
DNA sequence determination and analysis, expression in Escherichia coli strain JM109
-
DNA sequence determination and analysis, expression in Escherichia coli strain JM109
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation of enzyme denatured by urea, restores more than 90% of the original activity 60 min after dilution and after complete dialysis. Optimal temperature for refolding is 25°C
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
diagnostics
energy production
synthesis
analysis
-
usage for quantitative determination of glucose in clinical tests and in the food industry
analysis
-
use of glucose dehydrogenase in enzyme cycling method for measurement of allantoin in human serum
biotechnology
-
larger scale production of NAD(P)H in bioreactors by usage of the enzyme, a thermostable enzyme is advantageous
biotechnology
Escherichia coli transformants are prepared coexpressing the yeast reductase YOL151W and Bacillus GDH for the production of Ethyl (R, S)-4-chloro-3-hydroxybutanoate
biotechnology
-
azoreductase and glucose 1-dehydrogenase are coupled for both continuous generation of the cofactor NADH and azo dye removal. The results show that 85% maximum relative activity of azoreductase in an integrated enzyme system is obtained at the conditions: 1 U azoreductase: 10 U glucose 1-dehydrogenase, 250 mM glucose, 1.0 mM NAD+ and 150 microM methyl red
biotechnology
enzymatic reduction of the nicotinamide biomimetic cofactors 1-phenethyl-1,4-dihydropyridine-3-carboxamide using glucose dehydrogenase mutant I192T/V306I provides a regeneration system for artificial cofactors. The 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
biotechnology
-
production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day
biotechnology
-
(±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate
biotechnology
-
co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes
biotechnology
A0A068FPP9
the robust stability of the enzyme makes it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature
biotechnology
-
larger scale production of NAD(P)H in bioreactors by usage of the enzyme, a thermostable enzyme is advantageous
-
biotechnology
-
the robust stability of the enzyme makes it an attractive participant for cofactor regeneration on practical applications, especially for the catalysis implemented in acidic pH and high temperature
-
diagnostics
-
usage for quantitative determination of glucose in clinical tests and in the food industry
diagnostics
A0A068FPP9
the enzyme can be a potential diagnostic reagent for blood glucose measurement
diagnostics
-
the enzyme can be a potential diagnostic reagent for blood glucose measurement
-
energy production
-
NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
energy production
-
NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
energy production
-
NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices
synthesis
-
usage as NADP+ cofactor regenerator for enzymatic synthesis of chiral compounds such as ethyl-(S)-4-chloro-3-hydroxybutanoate and ethyl 4-chloro-3-oxobutanoate
synthesis
-
enzyme can be used for gluconic acid production in low water systems
synthesis
-
production of recombinant glucose 1-dehydrogenase in Escherichia coli, optimization of culture and induction conditions. Glucose 1-dehydrogenase is used to regenerate NADPH in vivo and in vitro and coupled with a NADPH-dependent bioreduction for efficient synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate from ethyl-4-chloro-3-oxobutanoate
synthesis
-
production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate, an important chiral intermediate for the synthesis of rosuvastatin, using carbonyl reductase coupled with glucose dehydrogenase. A recombinant Escherichia coli strain harboring carbonyl reductase R9M and glucose dehydrogenase is constructed with high carbonyl reduction activity and cofactor regeneration efficiency. The recombinant Escherichia coli cells are applied for the efficient production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate with a substrate conversion of 98.8%, a yield of 95.6% and an enantiomeric excess of more than 99.0% under 350 g/l of tert-butyl (S)-6-chloro-5-hydroxy-3-oxohexanoate after 12 h reaction. A substrate fed-batch strategy is further employed to increase the substrate concentration to 400 g/l resulting in an enhanced product yield to 98.5% after 12 h reaction in a 1 l bioreactor. Meanwhile, the space-time yield is 1182.3 g/l*day
synthesis
-
(±)-ethyl mandelate are important intermediates in the synthesis of numerous pharmaceuticals. Efficient routes for the production of these derivatives are highly desirable. A co-immobilization strategy is developed to overcome the issue of NADPH demand in the short-chain dehydrogenase/reductase (SDR) catalytic process. The SDR from Thermus thermophilus HB8 and the NAD(P)-dependent glucose dehydrogenase (GDH) from Thermoplasma acidophilum DSM 1728 are co-immobilized on silica gel. This dual-system offers an efficient route for the biosynthesis of (+/-)-ethyl mandelate
synthesis
glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application
synthesis
-
co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes
synthesis
Priestia megaterium AS1.223
-
production of recombinant glucose 1-dehydrogenase in Escherichia coli, optimization of culture and induction conditions. Glucose 1-dehydrogenase is used to regenerate NADPH in vivo and in vitro and coupled with a NADPH-dependent bioreduction for efficient synthesis of ethyl (R)-4-chloro-3-hydroxybutanoate from ethyl-4-chloro-3-oxobutanoate
-
synthesis
Priestia megaterium IWG3
-
glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
Crystallization and characterization of NADP-dependent D-glucose dehydrogenase from Gluconobacter suboxydans
Agric. Biol. Chem.
44
301-308
1980
Gluconobacter oxydans
-
brenda
Kataoka, M.; Rohani, L.P.S.; Wada, M.; Kita, K.; Yanase, H.; Urabe, I.; Shimizu, S.
Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system
Biosci. Biotechnol. Biochem.
62
167-169
1998
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Yamamoto, K.; Kurisi, G.; Kusunoki, M.; Tabata, S.; Urabe, I.; Osaki, S.
Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution
J. Biochem.
129
303-312
2001
Priestia megaterium, Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Bhaumik, S.R.; Sonawat, H.M.
Kinetic mechanism of glucose dehydrogenase from Halobacterium salinarum
Indian J. Biochem. Biophys.
36
143-149
1999
Halobacterium salinarum
brenda
Siebers, B.; Wendisch, V.F.; Hensel, R.
Carbohydrate metabolism in thermoproteus tenax: in vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase
Arch. Microbiol.
168
120-127
1997
Thermoproteus tenax
brenda
John, J.; Crennell, S.J.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum
Structure
15
385-393
1994
Thermoplasma acidophilum
-
brenda
Tranulis, M.A.; Christophersen, B.; Borrebaek, B.
Glucose dehydrogenase in beef (Bos taurus) and rainbow trout (Oncorhynchus mykiss) liver: a comparative study
Comp. Biochem. Physiol. B
109
427-435
1994
Bos taurus, Oncorhynchus mykiss
brenda
Nagao, T.; Mitamura, T.; Wang, X.H.; Negoro, S.; Yomo, T.; Urabe, I.; Okada, H.
Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isoenzymes from Bacillus megaterium IAM1030
J. Bacteriol.
174
5013-5020
1992
Priestia megaterium
brenda
Bright, J.R.; Mackness, R.; Danson, M.J.; Hough, D.W.; Taylor, G.L.; Towner, P.
Crystallization and preliminary crystallographic study of glucose dehydrogenase from the archaebacterium Thermoplasma acidophilum
J. Mol. Biol.
22
143-144
1991
Thermoplasma acidophilum
-
brenda
Hilt, W.; Pfleidere, G.; Fortnagel, P.
Glucose dehydrogenase from Bacillus subtilis expressed in Escherichia coli I: purification, characterization and comparison with glucose dehydrogenase from Bacillus megaterium
Biochim. Biophys. Acta
1076
298-304
1991
Bacillus subtilis
brenda
Persson, M.; Bulow, L.; Mosbach, K.
Purification and site-specific immobilization of genetically engineered glucose dehydrogenase on thiopropyl-sepharose
FEBS Lett.
270
41-44
1990
Bacillus subtilis
brenda
Yamamot, K.; Nagao, T.; Makino, Y.; Urabe, I.; Okada, H.
Characterization of mutant glucose dehydrogenase with increasing stability
Ann. N. Y. Acad. Sci.
613
362-365
1990
Priestia megaterium
brenda
Smith, L.D.; Budgen, N.; Bungard, S.J.; Danson, M.J.; Hough, D.W.
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
Biochem. J.
261
973-977
1989
Thermoplasma acidophilum
brenda
Carper, W.R.; Groutas, W.C.; Coffin, D.B.
Affinity chromatography of glucose dehydrogenase
Experientia
44
29-32
1988
Sus scrofa
brenda
Maurer, e.; Pfleiderer, G.
Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. II. Kinetics and mechanism
Z. Naturforsch. C
42
907-915
1987
Priestia megaterium
brenda
Hnes, J.; Jany, K.D.; Pfleiderer, G.; Wagner, A.F.V.
An integrated prediction of secondary, tertiary and quarternary structure of glucose dehydrogenase
FEBS Lett.
212
193-198
1987
Priestia megaterium
brenda
Giardina, P.; DeBasia, M.G.; DeRosa, M.; Gambacort, A.; Buonocore, V.
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
Biochem. J.
239
517-522
1986
Saccharolobus solfataricus
brenda
Juhasz, A.; Csizmadia, V.; Borbely, G.; Udvardy, J.; Farkas, G.L.
The pyridine nucleotide-dependent D-glucose dehydrogenase of Nostoc sp. strain Mac, a cyanobacterium, is subject to thioredoxin modulation
FEBS Lett.
194
121-125
1986
Nostoc sp., Nostoc sp. MAC
-
brenda
Maurer, E.; Pfleiderer, G.
Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. I. Conformational and functional changes
Biochim. Biophys. Acta
827
381-388
1985
Priestia megaterium
-
brenda
Strauss, N.
Role of glucose dehydrogenase in germination of Bacillus subtilis spores
FEMS Microbiol. Lett.
20
379-384
1983
Bacillus subtilis, Bacillus subtilis NS168I-2
-
brenda
Carper, W.R.; Campbell, D.P.; Morrical, S.W.; Thompson, R.E.
Characterization studies of glucose dehydrogenase
Experientia
39
1295-1297
1983
Sus scrofa
brenda
Ramaley, R.F.; Vasantha, N.
Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase
J. Biol. Chem.
258
12558-12565
1983
Bacillus subtilis
brenda
Thompson, R.E.; Morrical, S.W.; Campbell, D.P.; Carper, W.R.
Guanidinium- and temperature-induced conformational changes in glucose dehydrogenase
Biochim. Biophys. Acta
745
279-284
1983
Sus scrofa
brenda
Adachi, O.; Ameyama, M.
D-glucose dehydrogenase from Gluconobacter suboxydans
Methods Enzymol.
89
159-163
1982
Gluconobacter oxydans
-
brenda
Kobayashi, Y.; Ueyama, H.; Horikoshi, K.
Comparative studies of NAD+-dependent maltose dehydrogenase and D-glucose dehydrogenase produced by two strains of alkalophilic Corynebacterium species
Agric. Biol. Chem.
46
2139-2142
1982
Corynebacterium sp., Corynebacterium sp. 150-1, Corynebacterium sp. 93-1
-
brenda
Campbell, D.P.; Carper, W.R.; Thompson, R.E.
Bovine liver glucose dehydrogenase: isolation and characterization
Arch. Biochem. Biophys.
215
289-301
1982
Bos taurus
brenda
Kobayashi, Y.; Ueyama, H.; Horikoshi, K.
NAD-dependent maltose dehydrogenase and NAD-dependent D-glucose dehydrogenase of alkalophilic Corynebacterium sp. No. 150-1
Agric. Biol. Chem.
44
2837-2841
1980
Corynebacterium sp., Corynebacterium sp. 150-1
-
brenda
Kobayashi, Y.; Horikoshi, K.
Purification and properties of NAD-dependent D-glucose dehydrogenase produced by alkalophilic Crynebacterium sp. No. 93-1
Agric. Biol. Chem.
44
2261-2269
1980
Corynebacterium sp., Corynebacterium sp. 93-1
-
brenda
Yokota, A.; Sasajima, K.; Yoneda, M.
Reactivation of inactivated D-glucose dehydrogenase of a Bacillus species by pyridine and adenine nucleotides
Agric. Biol. Chem.
43
271-278
1979
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) BG 1722
-
brenda
Fujita, Y.; Ramaley, R.; Freese, E.
Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis
J. Bacteriol.
132
282-293
1977
Bacillus subtilis
brenda
Pauly, H.E.; Pfleiderer, G.
Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenase
Biochemistry
16
4599-4604
1977
Priestia megaterium
brenda
Pauly, H.E.; Pfleiderer, G.
D-Glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure
Hoppe-Seyler's Z. Physiol. Chem.
356
1613-1623
1975
Priestia megaterium
brenda
Pulich, W.M.; van Baalen, C.
Pyridine nucleotide-dependent glucose dehydrogenase activity in blue-green algae
J. Biol. Chem.
114
28-33
1973
Nostoc sp., Schizothrix calcicola, Lyngbya lagerheimii, Chlorogloeopsis fritschii
brenda
Shatton, J.B.; Halver, J.E.; Weinhouse, S.
Glucose (hexose 6-phosphate) dehydrogenase in liver of rainbow trout
J. Biol. Chem.
246
4878-4885
1971
Oncorhynchus mykiss
brenda
Thompson, R.E.; Carper, W.R.
Glucose dehydrogenase from pig liver. I. Isolation and purification
Biochim. Biophys. Acta
198
397-406
1970
Sus scrofa
brenda
Baik, S.H.; Ide, T.; Yoshida, H.; Kagami, O.; Harayama, S.
Significantly enhanced stability of glucose dehydrogenase by directed evolution
Appl. Microbiol. Biotechnol.
61
329-335
2003
Bacillus licheniformis, Bacillus subtilis, Priestia megaterium
brenda
Pire, C.; Marhuenda-Egea, F.C.; Esclapez, J.; Alcaraz, L.; Ferrer, J.; Bonete, M.J.
Stability and enzymatic studies of glucose dehydrogenase from the archaeon Haloferax mediterranei in reverse micelles
Biocatal. Biotransform.
22
17-23
2004
Haloferax mediterranei
-
brenda
Inose, K.; Fujikawa, M.; Yamazaki, T.; Kojima, K.; Sode, K.
Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli
Biochim. Biophys. Acta
1645
133-138
2003
Burkholderia cepacia (Q8GQE7)
brenda
Lamble, H.J.; Heyer, N.I.; Bull, S.D.; Hough, D.W.; Danson, M.J.
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
J. Biol. Chem.
278
34066-34072
2003
Saccharolobus solfataricus (O93715)
brenda
Ohshima, T.; Ito, Y.; Sakuraba, H.; Goda, S.; Kawarabayasi, Y.
The Sulfolobus tokodaii gene ST1704 codes highly thermostable glucose dehydrogenase
J. Mol. Catal. B
23
281-289
2003
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
-
brenda
Theodossis, A.; Milburn, C.C.; Heyer, N.I.; Lamble, H.J.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. F
F61
112-115
2005
Saccharolobus solfataricus
brenda
Yun, H.; Choi, H.L.; Fadnavis, N.W.; Kim, B.G.
Stereospecific synthesis of (R)-2-hydroxy carboxylic acids using recombinant E. coli BL21 overexpressing YiaE from Escherichia coli K12 and glucose dehydrogenase from Bacillus subtilis
Biotechnol. Prog.
21
366-371
2005
Bacillus subtilis
brenda
Sharma, V.; Kumar, V.; Archana, G.; Kumar, G.N.
Substrate specificity of glucose dehydrogenase (GDH) of Enterobacter asburiae PSI3 and rock phosphate solubilization with GDH substrates as C sources
Can. J. Microbiol.
51
477-482
2005
Enterobacter asburiae, Enterobacter asburiae PSI3
brenda
Luna, M.F.; Bernardelli, C.E.; Galar, M.L.; Boiardi, J.L.
Glucose metabolism in batch and continuous cultures of Gluconacetobacter diazotrophicus PAL 3
Curr. Microbiol.
52
163-168
2006
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL 3
brenda
Milburn, C.C.; Lamble, H.J.; Theodossis, A.; Bull, S.D.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Biol. Chem.
281
14796-14804
2006
Saccharolobus solfataricus (O93715)
brenda
Yamamoto, K.; Kusunoki, M.; Urabe, I.; Tabata, S.; Osaki, S.
Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Bacillus megaterium IWG3
Acta Crystallogr. Sect. D
56
1443-1445
2000
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Baik, S.H.; Michel, F.; Aghajari, N.; Haser, R.; Harayama, S.
Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state
Appl. Environ. Microbiol.
71
3285-3293
2005
Priestia megaterium (P40288), Priestia megaterium IGW3 (P40288)
brenda
Ulmer, W.; Froeschle, M.; Jany, K.D.
Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine
Eur. J. Biochem.
136
183-194
1983
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Froeschle, M.; Ulmer, W.; Jany, K.D.
Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state
Eur. J. Biochem.
142
533-540
1984
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Pal, G.P.; Jany, K.D.; Saenger, W.
Crystallization of and X-ray investigations on glucose dehydrogenase from Bacillus megaterium
Eur. J. Biochem.
167
123-124
1987
Priestia megaterium, Priestia megaterium MI286
brenda
Heilmann, H.J.; Maegert, H.J.; Gassen, H.G.
Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coli
Eur. J. Biochem.
174
485-490
1988
Priestia megaterium, Priestia megaterium M1286
brenda
Mitamura, T.; Urabe, I.; Okada, H.
Enzymatic properties of isozymes and variants of glucose dehydrogenase from Bacillus megaterium
Eur. J. Biochem.
186
389-393
1989
Priestia megaterium, Priestia megaterium (P40288), Priestia megaterium (P39482), Priestia megaterium IAM 1030, Priestia megaterium IAM 1030 (P39482), Priestia megaterium IWG3 (P40288)
brenda
Makino, Y.; Negoro, S.; Urabe, I.; Okada, H.
Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3
J. Biol. Chem.
264
6381-6385
1989
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Kanaujia, S.P.; Ranjani, C.V.; Jeyakanthan, J.; Nishida, M.; Kitamura, Y.; Baba, S.; Ebihara, A.; Shimizu, N.; Nakagawa, N.; Shinkai, A.; Yamamoto, M.; Kuramitsu, S.; Shiro, Y.; Sekar, K.; Yokoyama, S.
Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8
Acta Crystallogr. Sect. F
63
446-448
2007
Thermus thermophilus HB8
brenda
Muratsubaki, H.; Enomoto, K.; Soejima, A.; Satake, K.
An enzyme cycling method for measurement of allantoin in human serum
Anal. Biochem.
378
65-70
2008
Priestia megaterium
brenda
Vazquez-Figueroa, E.; Chaparro-Riggers, J.; Bommarius, A.S.
Development of a thermostable glucose dehydrogenase by a structure-guided consensus concept
ChemBioChem
8
2295-2301
2007
Bacillus licheniformis, Bacillus subtilis subsp. subtilis, Bacillus subtilis subsp. subtilis 168, Bacillus thuringiensis
brenda
Xu, Z.; Jing, K.; Liu, Y.; Cen, P.
High-level expression of recombinant glucose dehydrogenase and its application in NADPH regeneration
J. Ind. Microbiol. Biotechnol.
34
83-90
2007
Priestia megaterium, Priestia megaterium AS1.223
brenda
Senesi, S.; Csala, M.; Marcolongo, P.; Fulceri, R.; Mandl, J.; Banhegyi, G.; Benedetti, A.
Hexose-6-phosphate dehydrogenase in the endoplasmic reticulum
Biol. Chem.
391
1-8
2010
Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Ding, H.T.; Du, Y.Q.; Liu, D.F.; Li, Z.L.; Chen, X.J.; Zhao, Y.H.
Cloning and expression in E. coli of an organic solvent-tolerant and alkali-resistant glucose 1-dehydrogenase from Lysinibacillus sphaericus G10
Biores. Technol.
102
1528-1536
2010
Lysinibacillus sphaericus (C5IFU0), Lysinibacillus sphaericus G10 (C5IFU0), Lysinibacillus sphaericus G10
brenda
Alcina, A.; Ramagopalan, S.V.; Fernandez, O.; Catala-Rabasa, A.; Fedetz, M.; Ndagire, D.; Leyva, L.; Arnal, C.; Delgado, C.; Lucas, M.; Izquierdo, G.; Ebers, G.C.; Matesanz, F.
Hexose-6-phosphate dehydrogenase: a new risk gene for multiple sclerosis
Eur. J. Hum. Genet.
18
618-620
2010
Homo sapiens
brenda
Gomez-Sanchez, E.P.; Gomez-Sanchez, M.T.; de Rodriguez, A.F.; Romero, D.G.; Warden, M.P.; Plonczynski, M.W.; Gomez-Sanchez, C.E.
Immunohistochemical demonstration of the mineralocorticoid receptor, 11beta-hydroxysteroid dehydrogenase-1 and -2, and hexose-6-phosphate dehydrogenase in rat ovary
J. Histochem. Cytochem.
57
633-641
2009
Rattus norvegicus
brenda
Rogoff, D.; Black, K.; McMillan, D.R.; White, P.C.
Contribution of hexose-6-phosphate dehydrogenase to NADPH content and redox environment in the endoplasmic reticulum
Redox Rep.
15
64-70
2010
Mus musculus
brenda
Haferkamp, P.; Kutschki, S.; Treichel, J.; Hemeda, H.; Sewczyk, K.; Hoffmann, D.; Zaparty, M.; Siebers, B.
An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?
Biochem. Soc. Trans.
39
77-81
2011
Saccharolobus solfataricus (Q97U21)
brenda
Yang, Y.; Wei, B.; Zhao, Y.; Wang, J.
Construction of an integrated enzyme system consisting azoreductase and glucose 1-dehydrogenase for dye removal
Biores. Technol.
130
517-521
2013
Lysinibacillus sphaericus
brenda
Nishioka, T.; Yasutake, Y.; Nishiya, Y.; Tamura, T.
Structure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1-dehydrogenase IV
FEBS J.
279
3264-3275
2012
Priestia megaterium, Priestia megaterium (P39485)
brenda
Park, H.J.; Jung, J.; Choi, H.; Uhm, K.N.; Kim, H.K.
Enantioselective bioconversion using Escherichia coli cells expressing Saccharomyces cerevisiae reductase and Bacillus subtilis glucose dehydrogenase
J. Microbiol. Biotechnol.
20
1300-6
2010
Bacillus subtilis (A6N8S2)
brenda
Britton, K.L.; Baker, P.J.; Fisher, M.; Ruzheinikov, S.; Gilmour, D.J.; Bonete, M.J.; Ferrer, J.; Pire, C.; Esclapez, J.; Rice, D.W.
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
Haloferax mediterranei (Q977U7), Haloferax mediterranei DSM 1411 (Q977U7)
brenda
Haferkamp, P.
Biochemical studies of enzymes involved in glycolysis of the thermoacidophilic crenarchaeon Sulfolobus solfataricus
PH. D. Thesis Universitt Duisburg-Essen
2011
0000
2011
Saccharolobus solfataricus (Q97U21), Saccharolobus solfataricus DSM 1617 (Q97U21)
-
brenda
Pongtharangkul, T.; Chuekitkumchorn, P.; Suwanampa, N.; Payongsri, P.; Honda, K.; Panbangred, W.
Kinetic properties and stability of glucose dehydrogenase from Bacillus amyloliquefaciens SB5 and its potential for cofactor regeneration
AMB Express
5
68
2015
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens SB5
brenda
Yu, T.; Li, J.; Zhu, L.; Hu, D.; Deng, C.; Cai, Y.; Wu, M.
Reduction of m-chlorophenacyl chloride coupled with regeneration of NADPH by recombinant Escherichia coli cells co-expressing both carbonyl reductase and glucose 1-dehydrogenase
Ann. Microbiol.
66
343-350
2016
Thermoplasma acidophilum
-
brenda
Gao, F.; Ding, H.; Xu, X.; Zhao, Y.
A self-sufficient system for removal of synthetic dye by coupling of spore-displayed triphenylmethane reductase and glucose 1-dehydrogenase
Environ. Sci. Pollut. Res. Int.
23
21319-21326
2016
Bacillus subtilis
brenda
Ding, H.; Gao, F.; Liu, D.; Li, Z.; Xu, X.; Wu, M.; Zhao, Y.
Significant improvement of thermal stability of glucose 1-dehydrogenase by introducing disulfide bonds at the tetramer interface
Enzyme Microb. Technol.
53
365-372
2013
Lysinibacillus sphaericus (C5IFU0), Lysinibacillus sphaericus G10 (C5IFU0)
brenda
Lu, L.; Yang, Y.; Lin, H.; Gao, F.; Zhao, Y.
Construction, expression and characterization of fusion enzyme containing azoreductase and glucose 1-dehydrogenase for dye removal
Int. Biodeter. Biodegrad.
87
81-86
2014
Lysinibacillus sphaericus (C5IFU0), Lysinibacillus sphaericus G10 (C5IFU0)
-
brenda
Hyun, J.; Abigail, M.; Choo, J.W.; Ryu, J.; Kim, H.K.
Effects of N-/C-terminal extra tags on the optimal reaction conditions, activity, and quaternary structure of Bacillus thuringiensis glucose 1-dehydrogenase
J. Microbiol. Biotechnol.
26
1708-1716
2016
Bacillus thuringiensis serovar kurstaki, Bacillus thuringiensis serovar kurstaki KCCM 11429
brenda
Nowak, C.; Pick, A.; Lommes, P.; Sieber, V.
Enzymatic reduction of nicotinamide biomimetic cofactors using an engineered glucose dehydrogenase providing a regeneration system for artificial cofactors
ACS Catal.
7
5202-5208
2017
Saccharolobus solfataricus (O93715)
-
brenda
Stolarczyk, K.; Rogalski, J.; Bilewicz, R.
NAD(P)-dependent glucose dehydrogenase applications for biosensors, bioelectrodes, and biofuel cells
Bioelectrochemistry
135
107574
2020
Priestia megaterium, Thermoplasma acidophilum, Aspergillus niger
-
brenda
Zhang, X.; Zheng, L.; Wu, D.; Zhou, R.; Liu, Z.; Zheng, Y.
Production of tert-butyl (3R,5S)-6-chloro-3,5-dihydroxyhexanoate using carbonyl reductase coupled with glucose dehydrogenase with high space-time yield
Biotechnol. Prog.
36
e2900
2020
Exiguobacterium artemiae
brenda
Liu, X.; Du, X.; Feng, J.; Wu, M.; Lin, J.; Guan, J.; Wang, T.; Zhang, Z.
Co-immobilization of short-chain dehydrogenase/reductase and glucose dehydrogenase for the efficient production of ()-ethyl mandelate
Catal. Lett.
149
1710-1720
2019
Thermoplasma acidophilum
-
brenda
Qian, W.; Ou, L.; Li, C.; Pan, J.; Xu, J.; Chen, Q.; Zheng, G.
Evolution of glucose dehydrogenase for cofactor regeneration in bioredox processes with denaturing agents
ChemBioChem
21
2680-2688
2020
Priestia megaterium (P40288), Priestia megaterium IWG3 (P40288)
brenda
Plz, M.; Petrovicova, T.; Rebros, M.
Semi-continuous flow biocatalysis with affinity co-immobilized ketoreductase and glucose dehydrogenase
Molecules
25
4278
2020
Priestia megaterium
brenda
Ding, H.; Gao, F.; Yu, Y.; Chen, B.
Biochemical and computational insights on a novel acid-resistant and thermal-stable glucose 1-dehydrogenase
Int. J. Mol. Sci.
18
1198
2017
Bacillus sp. (in: firmicutes) (A0A068FPP9), Bacillus sp. (in: firmicutes) ZJ (A0A068FPP9)
brenda
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