HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.47
Word Map on EC 1.1.1.47
- 1.1.1.47
-
glucocorticoid
- 11beta-hydroxysteroid
- glucose-6-phosphate
- cortisone
- corticosterone
- 11beta-hsd1
- hsd11b1
- 11-dehydrocorticosterone
-
oxo-reductase
-
prereceptor
-
digenic
- diagnostics
- biotechnology
- synthesis
- analysis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.1.1.47
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase [NAD(P)+]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
ordered bi bi mechanism, formation of ternary complexes, NADP+ adds first, NADPH formed dissociates last, for reverse reaction, NADPH adds first, NADP+ leaves last
-
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
ordered bi bi mechanism
-
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential type ordered bibi mechnanism
-
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential ordered bi-bi mechanism
-
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
sequential ordered bi-bi mechanism
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-53-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain IWG3
UniProt
-
-
-
strain IWG3
UniProt
Please 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 Entner–Doudoroff pathway
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
5% of the activity with D-glucose and NAD+
-
-
?
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+
-
66% of the activity with D-glucose
-
-
?
6-deoxy-D-glucose + NADP+
? + NADPH
-
9% of the activity with D-glucose and NAD+
-
-
?
beta-D-galactose + 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
-
-
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+
-
-
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+
-
-
ir
beta-D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
-
8% of the activity with D-glucose
-
-
?
D-allose + NADP+
D-allono-1,5-lactone + NADPH
-
13% of the activity with D-glucose and NAD+
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
-
5% of the activity with D-glucose
-
-
?
D-altrose + NADP+
D-altrono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-fructose + NAD(P)+
? + NAD(P)H
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-fructose + NADP+
?
-
0.03% activity compared to D-glucose
-
-
?
D-galactose + NADP+
?
-
1.09% activity compared to D-glucose
-
-
?
D-gulose + NAD+
D-gulono-1,5-lactone + NADH
-
8% of the activity with D-glucose
-
-
?
D-gulose + NADP+
D-gulono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-idose + NAD+
D-idono-1,5-lactone + NADH
-
65% of the activity with D-glucose
-
-
?
D-idose + NADP+
D-idono-1,5-lactone + NADPH
-
12% of the activity with D-glucose and NAD+
-
-
?
D-lactose + NAD+
D-lactono-1,5-lactone + NADH + H+
relative activity: 4.2%
-
-
?
D-lactose + NADP+
?
-
3.0% activity compared to D-glucose
-
-
?
D-maltose + NADP+
?
-
1.03% activity compared to D-glucose
-
-
?
D-mannose + NADP+
?
-
11.53% activity compared to D-glucose
-
-
?
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
-
4% of the activity with D-glucose and NADP+
-
-
?
D-xylose + NADP+
?
-
12.89% activity compared to D-glucose
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
14% of the activity with D-glucose
-
-
?
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
26% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
114% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
112% relative activity
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
112% relative activity
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
113% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
Bacillus sp. BG 1722
-
113% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
108% of the activity with D-glucose
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
12% of the activity with glucose
-
-
?
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+
-
103% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. BG 1722
-
103% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
25% of the activity with D-glucose and NAD+
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
low activity
-
-
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
-
-
-
-
?
beta-D-glucose + 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+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
enzyme plays a role in germination
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
multifunctional enzyme is involved in several catabolic sugar pathways in the endoplasmic reticulum
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
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+
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+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
velocities of the reverse reaction at pH 7.0 and 8.0 are 2.2% and 5.9% respectively, of the oxidative reaction
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
5.9% velocity for reverse reaction compared to forward reaction at pH 8.0
-
-
r
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
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+
-
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+
-
-
-
-
?
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+
-
93% of the activity with NAD+
-
-
?
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Bacillus sp. 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+
-
-
-
-
?
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+
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-fructose + NAD+
? + NADH
-
9% of the activity with D-glucose
-
-
?
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+
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 + 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 + 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(P)+
D-glucono-1,5-lactone + NAD(P)H
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% relative activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
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+
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+
C5IFUO
-
-
-
?
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+
-
75% relative activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
75% relative activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose + 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+
C5IFUO
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
C5IFUO
-
-
-
?
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
-
2% relative activity
-
-
?
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 + NAD+
D-mannono-1,5-lactone + NADH + H+
relative activity: 7.6%
-
-
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
88% of the activity with D-glucose
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
wild-type and mutant enzymes
-
-
?
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+
-
44% of the activity with D-glucose
-
-
-
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
47% of the activity with D-glucose
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
44% of the activity with D-glucose
-
-
-
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
relative activity: 22.5%
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
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
-
-
?
gentiobiose + NAD+
? + NADH
-
103% of the activity with gentiobiose
-
-
?
gentiobiose + NAD+
? + NADH
-
103% of the activity with gentiobiose
-
-
?
additional information
?
-
-
no activity of wild-type and mutant enzymes with sucrose
-
-
-
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
-
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
-
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
-
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
-
additional information
?
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
-
additional information
?
-
-
no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol
-
-
-
additional information
?
-
-
no activity with D-galactose, D-ribose, D-fructose, and myo-inositol with NAD+ as the cosubstrate
-
-
-
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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q97U21
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+
Q97U21
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+
O93715
first step of the non-phosphorylative Entner-Doudoroff pathway
-
-
ir
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+
C5IFUO
-
-
-
?
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+
C5IFUO
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
C5IFUO
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
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+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
NAD+
-
-
285784, 639095, 639105, 639108, 639109, 639126, 654301, 677305, 677657, 679607, 679608, 679611, 679613, 679615, 680592
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+; kcat/Km of glucose in reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+
NADP+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
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+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
NADP+
-
-
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+; kcat/Km of glucose in reaction with NADP+ is about 8fold higher compared to kcat/Km of glucose in the reaction with NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Mg2+
Mn2+
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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+
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
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
2000
D-glucose
pH 8.0, 37°C, mutant DELTAG261; pH 8.0, 37°C, mutant G261A
4000
D-glucose
pH 6.0, 37°C, mutant G261V; pH 8.0, 37°C, mutant G259V
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
0.22
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
2.23
NAD+
-
cosubstrate D-glucose, 70°C, pH not specified in the publication
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; 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
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
190
D-glucose
isozyme GlcDH-I; isozyme GlcDH-I; isozyme GlcDH-I; isozyme GlcDH-II; isozyme GlcDH-II; isozyme GlcDH-II
317
D-glucose
apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
334
D-glucose
apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
352
D-glucose
apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
390
D-glucose
isozyme GlcDH-IWG3; isozyme GlcDH-IWG3; isozyme GlcDH-IWG3
395
D-glucose
apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
beta-D-glucose as substrate and D-galactose as carbon source; beta-D-glucose as the sole carbon source and D-cellobiose as substrate
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