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Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
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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+).
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
alkali-resistant glucose 1-dehydrogenase, beta-D-glucose:NAD(P)+ 1-oxido-reductase, beta-D-glucose:NAD(P)+ 1-oxidoreductase, BmGlcDH-III, BmGlcDH-IV, D-glucose dehydrogenase (NAD(P)), EC 1.1.5.2, GDH, gdh-2, GDHB, 
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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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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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hexose-6-phosphate dehydrogenase
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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+
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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+
sequential ordered bi-bi mechanism
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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+
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
BRENDA
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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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5% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-beta-D-xylose + NAD+
2-deoxy-D-xylono-1,5-lactone + NADH + H+
-
-
-
-
r
2-deoxy-D-glucose 6-phosphate + NAD+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADH
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
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66% of the activity with D-glucose
-
-
?
6-deoxy-D-glucose + NADP+
? + NADPH
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9% of the activity with D-glucose and NAD+
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
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ir
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
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-
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
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ir
beta-D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
beta-D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
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26% activity compared to D-glucose
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r
D-allose + NAD+
D-allono-1,5-lactone + NADH
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8% of the activity with D-glucose
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?
D-allose + NADP+
D-allono-1,5-lactone + NADPH
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13% of the activity with D-glucose and NAD+
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?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
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5% of the activity with D-glucose
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?
D-altrose + NADP+
D-altrono-1,5-lactone + NADPH
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12% of the activity with D-glucose and NAD+
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-
?
D-fructose + NAD(P)+
? + NAD(P)H
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no activity with mutants Q252L and Q252L/E170K
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?
D-fructose + NADP+
?
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0.03% activity compared to D-glucose
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-
?
D-galactose + NADP+
?
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1.09% activity compared to D-glucose
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-
?
D-galactose 6-phosphate + NAD+
6-phospho-D-galactono-1,5-lactone + NADH + H+
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-
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r
D-galactose 6-phosphate + NADP+
6-phospho-D-galactono-1,5-lactone + NADPH + H+
-
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r
D-glucose + 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
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-
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?
D-glucose + 1-benzyl-3-carbamoylpyridin-1-ium chloride
D-glucono-1,5-lactone + reduced 1-benzyl-3-carbamoylpyridin-1-ium chloride
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-
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?
D-glucose + 1-phenethyl-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-phenethyl-1,4-dihydropyridine-3-carboxamide
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?
D-gulose + NAD+
D-gulono-1,5-lactone + NADH
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8% of the activity with D-glucose
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?
D-gulose + NADP+
D-gulono-1,5-lactone + NADPH
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12% of the activity with D-glucose and NAD+
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?
D-idose + NAD+
D-idono-1,5-lactone + NADH
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65% of the activity with D-glucose
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?
D-idose + NADP+
D-idono-1,5-lactone + NADPH
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12% of the activity with D-glucose and NAD+
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?
D-lactose + NAD+
D-lactono-1,5-lactone + NADH + H+
relative activity: 4.2%
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?
D-lactose + NADP+
?
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3.0% activity compared to D-glucose
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?
D-maltose + NADP+
?
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1.03% activity compared to D-glucose
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?
D-mannose + NADP+
?
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11.53% activity compared to D-glucose
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?
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
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4% of the activity with D-glucose and NADP+
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?
D-xylose + NADP+
?
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12.89% activity compared to D-glucose
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?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
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14% of the activity with D-glucose
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?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
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26% of the activity with D-glucose
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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113% of the activity with D-glucose
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Bacillus sp. (in: Bacteria) BG 1722
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113% of the activity with D-glucose
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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108% of the activity with D-glucose
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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-
-
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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114% of the activity with D-glucose
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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112% relative activity
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Priestia megaterium M1286
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112% relative activity
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?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
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12% of the activity with glucose
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?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
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103% of the activity with D-glucose and NAD+
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?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. (in: Bacteria) BG 1722
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103% of the activity with D-glucose and NAD+
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-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
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25% of the activity with D-glucose and NAD+
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-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
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-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
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low activity
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?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
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-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
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enzyme plays a role in germination
-
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?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
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enzyme plays a role in germination
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?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
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multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
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ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
best substrate, wild-type and mutant enzymes
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
first step of the non-phosphorylative Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
9% of the activity with NAD+
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km for glucose in the reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
93% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. (in: Bacteria) BG 1722
-
93% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
1% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
1% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
in the reverse reaction only 4% of the reaction occurs at neutral pH
-
-
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
-
-
r
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
about 3times more active with NADP+ than with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is highly specific for beta-D-glucose
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km of NADP+ is about 8fold higher compared to kcat/Km of NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km of glucose in the reaction with NADP+ is about 8fold higher compared to kcat/Km of glucose in reaction with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100fold higher affinity for NADP+ than for NAD+
-
-
ir
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
low activity with wild-type and mutant enzymes
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
equally active compared to beta-D-glucose
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
15% of the activity with D-glucose and NAD+
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
relative activity: 17.3%
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
relative activity: 17.3%
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 2.9% (reference: D-glucose 100%)
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 9.1% (reference: D-glucose 100%)
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
5% of the activity with D-glucose
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 11% (reference: D-glucose 100%)
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 3% (reference: D-glucose 100%)
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
relative activity: 100%
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
about 20% activity with D-galactose, D-xylose, maltose
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
relative activity: 100%
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
about 20% activity with D-galactose, D-xylose, maltose
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
Priestia megaterium M1286
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100% activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
100% activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
75% relative activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Priestia megaterium M1286
-
75% relative activity
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
other substrates: hexose-6-phosphates, glucose-6-sulfate, glucose
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
-
2% relative activity
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
Priestia megaterium M1286
-
2% relative activity
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
relative activity: 7.6%
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 18% (reference: D-glucose 100%)
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 4.8% (reference: D-glucose 100%)
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
88% of the activity with D-glucose
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
no activity
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
wild-type and mutant enzymes
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
44% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Corynebacterium sp. 150-1
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
44% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 10% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
substrate specificity wild-tpye: 35% (reference: D-glucose 100%)
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
28% of the activity with D-glucose and NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
28% of the activity with D-glucose and NAD+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
gentiobiose + NAD+
? + NADH
-
103% of the activity with gentiobiose
-
-
?
maltose + NAD+
? + NADH
-
6% of the activity with D-glucose
-
-
?
maltose + NAD+
? + NADH
Bacillus sp. (in: Bacteria) BG 1722
-
6% of the activity with D-glucose
-
-
?
maltose + NADP+
? + NADPH
-
5% of the activity D-glucose and NAD+
-
-
?
maltose + NADP+
? + NADPH
Bacillus sp. (in: Bacteria) BG 1722
-
5% of the activity D-glucose and NAD+
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
Cys residues are not involved in the catalytic site
-
-
?
additional information
?
-
-
no activity of wild-type and mutant enzymes with sucrose
-
-
?
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
Priestia megaterium IAM 1030
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
Priestia megaterium IAM 1030
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
Priestia megaterium IWG3
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
?
additional information
?
-
Priestia megaterium M1286
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
?
additional information
?
-
D-ribose, maltose, lactose and sucrose are poor substrates, no activity with D-allose, D-arabinose, and D-mannose
-
-
?
additional information
?
-
no substrates: D-allose, D-mannose, L-arabinose, D-ribose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose, ethanol
-
-
?
additional information
?
-
no substrates: D-allose, D-mannose, L-arabinose, D-ribose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose, ethanol
-
-
?
additional information
?
-
-
broad substrate specificity, no activity with D-mannose, D-ribose, and glucose 6-phosphate, cofactor specificity depends on the sugar sustrate
-
-
?
additional information
?
-
-
broad substrate specificity, no activity with D-mannose, D-ribose, and glucose 6-phosphate, cofactor specificity depends on the sugar sustrate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
GDH-2 is absolutely specific for D-glucose. D-galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol were not used as substrates. kcat/Km of NADP+ is about 8fold higher compared to kcat/Km of NAD+
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
first step of the non-phosphorylative Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
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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+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
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+
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, 65°C, pH not specified in the publication
0.15
NADP+
cosubstrate D-glucose, 80°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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