Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.47
-
RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase [NAD(P)+]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
Entner Doudoroff pathway
-
-
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+).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-53-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain IGW3
UniProt
Manually annotated by BRENDA team
strain M1286
-
-
Manually annotated by BRENDA team
strain MI286
-
-
Manually annotated by BRENDA team
strain BG 1722, D-ribose producing mutant
-
-
Manually annotated by BRENDA team
Bacillus sp. BG 1722
strain BG 1722, D-ribose producing mutant
-
-
Manually annotated by BRENDA team
strain NS168I-2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
FERM BP-7306 strain SM-4
SwissProt
Manually annotated by BRENDA team
strain 150-1
-
-
Manually annotated by BRENDA team
strain 93-1
-
-
Manually annotated by BRENDA team
strain PSI3
-
-
Manually annotated by BRENDA team
strain PSI3
-
-
Manually annotated by BRENDA team
strain PAL 3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MAC
-
-
Manually annotated by BRENDA team
strain 7, JCM 10545, gene ST1704
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-
Manually annotated by BRENDA team
strain 7, JCM 10545, gene ST1704
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
identification (single-nucleotide polymorphism) of hexose-6-phosphate dehydrogenase as a risk gene for multiple sclerosis
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxy-D-glucose + NAD(P)+
?
show the reaction diagram
2-amino-2-deoxy-D-glucose + NAD+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
2-amino-2-deoxy-D-glucose + NADP+
2-amino-2-deoxy-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
5% of the activity with D-glucose and NAD+
-
-
?
2-deoxy-D-glucose + NAD(P)+
?
show the reaction diagram
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
2-deoxy-D-glucose + NAD+
?
show the reaction diagram
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
2-deoxy-D-glucose 6-phosphate + NAD+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADH
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
6-deoxy-D-glucose + NAD(P)+
?
show the reaction diagram
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
66% of the activity with D-glucose
-
-
?
6-deoxy-D-glucose + NADP+
? + NADPH
show the reaction diagram
-
9% of the activity with D-glucose and NAD+
-
-
?
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
beta-D-glucose + 2,6-dichlorophenol-indophenol
?
show the reaction diagram
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
show the reaction diagram
the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH
show the reaction diagram
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
-
-
ir
beta-D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
show the reaction diagram
the enzyme is absolutely specific for glucose. D-Galactose, D-allose, D-mannose, D-xylose, L-arabinose, D-ribose, D-xylose, D-arabinose, L-xylose, D-glucosamine, 2-deoxy-D-glucose, D-fucose, D-lactose, D-maltose, D-fructose and ethanol are not used as substrates. the catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
-
-
ir
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
beta-D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
beta-D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
cellobiose + NAD+
? + NADH
show the reaction diagram
D-allose + NAD(P)+
?
show the reaction diagram
-
low activity
-
-
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
show the reaction diagram
-
8% of the activity with D-glucose
-
-
?
D-allose + NADP+
D-allono-1,5-lactone + NADPH
show the reaction diagram
-
13% of the activity with D-glucose and NAD+
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
show the reaction diagram
-
5% of the activity with D-glucose
-
-
?
D-altrose + NADP+
?
show the reaction diagram
-
low activity
-
-
?
D-altrose + NADP+
D-altrono-1,5-lactone + NADPH
show the reaction diagram
-
12% of the activity with D-glucose and NAD+
-
-
?
D-cellobiose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
D-fructose + NAD(P)+
? + NAD(P)H
show the reaction diagram
-
no activity with mutants Q252L and Q252L/E170K
-
-
?
D-fructose + NAD+
?
show the reaction diagram
D-fructose + NAD+
? + NADH
show the reaction diagram
D-fucose + NAD(P)+
?
show the reaction diagram
-
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
show the reaction diagram
D-galactose + NAD+
?
show the reaction diagram
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
show the reaction diagram
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
show the reaction diagram
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
D-glucosamine + NAD(P)+
?
show the reaction diagram
low activity
-
-
?
D-glucosamine + NAD+
?
show the reaction diagram
-
-
-
?
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH
show the reaction diagram
D-glucosamine + NAD+
D-glucosamino-1,5-lactone + NADH + H+
show the reaction diagram
D-glucosamine + NADP+
D-glucosamino-1,5-lactone + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H
show the reaction diagram
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
D-gulose + NAD(P)+
?
show the reaction diagram
-
low activity
-
-
?
D-gulose + NAD+
D-gulono-1,5-lactone + NADH
show the reaction diagram
-
8% of the activity with D-glucose
-
-
?
D-gulose + NADP+
D-gulono-1,5-lactone + NADPH
show the reaction diagram
-
12% of the activity with D-glucose and NAD+
-
-
?
D-idose + NAD(P)+
?
show the reaction diagram
low activity
-
-
?
D-idose + NAD+
D-idono-1,5-lactone + NADH
show the reaction diagram
-
65% of the activity with D-glucose
-
-
?
D-idose + NADP+
D-idono-1,5-lactone + NADPH
show the reaction diagram
-
12% of the activity with D-glucose and NAD+
-
-
?
D-lactose + NAD+
D-lactono-1,5-lactone + NADH + H+
show the reaction diagram
relative activity: 4.2%
-
-
?
D-lyxose + NAD(P)+
?
show the reaction diagram
low activity
-
-
?
D-maltose + NAD(P)+
? + NAD(P)H
show the reaction diagram
D-maltose + NAD+
?
show the reaction diagram
relative activity: 22.4%
-
-
?
D-mannose + NAD(P)+
? + NAD(P)H
show the reaction diagram
D-mannose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-mannose + NAD+
D-mannono-1,5-lactone + NADH
show the reaction diagram
D-mannose + NAD+
D-mannono-1,5-lactone + NADH + H+
show the reaction diagram
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
show the reaction diagram
D-ribose + NADP+
?
show the reaction diagram
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
show the reaction diagram
-
4% of the activity with D-glucose and NADP+
-
-
?
D-xylose + NAD(P)+
?
show the reaction diagram
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
D-xylose + NAD+
?
show the reaction diagram
weak substrate
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
show the reaction diagram
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
gentiobiose + NAD+
? + NADH
show the reaction diagram
gluconate + NAD+
? + NADH
show the reaction diagram
L-arabinose + NAD(P)+
?
show the reaction diagram
maltose + NAD+
? + NADH
show the reaction diagram
maltose + NADP+
? + NADPH
show the reaction diagram
sucrose + NAD+
?
show the reaction diagram
relative activity: 6.3%
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + NAD(P)(+)
D-glucono-1,5-lactone + NAD(P)H
show the reaction diagram
Q97U21
the enzyme might represent the major player in glucose catabolism via the branched Entner-Doudoroff pathway
-
-
ir
beta-D-glucose + NAD(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
beta-D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
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+
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the catalytic alpha-subunit contains a FAD binding motif at the N-terminal region
NADPH
additional information
-
dual cofactor specificity due to presence of Asn215, His217, and the GXGXXA motif
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
Ca2+
-
maximal activity at 20 mM
Cd2+
inhibits enzymatic activity
Co2+
inhibits enzymatic activity
Cu2+
inhibits enzymatic activity
EDTA
enhances activity
Fe2+
inhibits enzymatic activity
Fe3+
inhibits enzymatic activity
K+
50-200 mM, Tris/HCl buffer pH 9.0; enhances activity
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+
50-200 mM, Tris/HCl buffer pH 9.0; enhances activity
MgCl2
-
25 mM for activity assay
Na+
50-200 mM, Tris/HCl buffer pH 9.0; enhances activity
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
NH4+
50-200 mM, Tris/HCl buffer pH 9.0; enhances activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
1 M, 71% inhibition
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
Ag+
-
1 mM, 99% inhibition
Cd2+
more than 50% inhibition at 20 mM
D-glucono-1,5-lactone
-
forward reaction, oxidation, product inhibition, noncompetitive vs. beta-D-glucose and NADP+
dithiothreitol
-
10 mM, 28% inhibition
KCl
-
1 M, 44% inhibition
LiCl
-
1 M, 64% inhibition
N-ethylmaleimide
-
3 mM, room temperature, pH 9.0, 50% inactivation
NAD+
-
above 12 mM
NADH
-
0.1 mM, 45% inhibition, noncompetitive inhibitorr of D-glucose
NADP+
NADPH
p-chloromercuribenzoate
-
1 mM, 93% inhibition
Tetranitromethane
-
the rapid inactivation can be prevented by the presence of NAD, AMP, or ATP
thioredoxin
-
in the presence of 0.5 mM dithiothreitol
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
EDTA
10-100 mM, sodium phosphate buffer, pH 8.0
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
NADP+
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
47.8
2-deoxy-beta-D-glucose
-
pH 7.8, 23°C
4.2
2-deoxy-D-glucose
-
pH 6.5
0.3 - 25
2-deoxy-D-glucose 6-phosphate
9.8 - 11
4-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
3.2 - 5.6
6-O-(beta-D-glucopyranosido)-beta-D-glucopyranoside
0.44 - 204
beta-D-galactose
0.0024 - 135
beta-D-glucose
68
beta-D-xylose
-
pH 9.0, 70°C, coenzyme NAD+
11
cellobiose
-
pH 9.8
800 - 10000
D-galactose
0.04 - 5
D-galactose 6-phosphate
35
D-glucosamine
-
pH 6.5
0.17 - 5000
D-glucose
0.0015 - 0.1
D-glucose 6-phosphate
0.0029 - 0.0083
D-Glucose-6-phosphate
0.18 - 200
D-xylose
0.01
galactose 6-phosphate
-
pH 7.5, 25°C, coenzyme NADP+
3.2
gentiobiose
-
pH 9.8
0.0003 - 48
NAD+
0.0036 - 105
NADP+
8
xylose
-
pH 7.0, 70°C
additional information
additional information
-
steady-state kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7 - 61
beta-D-galactose
4 - 802
beta-D-glucose
11.1 - 395
D-glucose
1.5 - 14.2
D-glucose 6-phosphate
7 - 81
D-xylose
23 - 390
NAD+
18 - 300
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.86 - 115.2
beta-D-glucose
96
14.86 - 115.2
D-glucose
35
9.74 - 31.95
NAD+
7
178.3 - 294.5
NADP+
10
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
3-(2-bromoacetyl)pyridine
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.22
-
beta-D-glucose as substrate and D-cellobiose as carbon source
0.26
-
beta-D-glucose as substrate and D-mannose as carbon source
0.27
-
-
0.28
-
beta-D-glucose as substrate and D-maltose as carbon source
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)
0.37
-
beta-D-glucose as substrate and D-xylose as carbon source
0.38
-
beta-D-glucose as the sole carbon source and a mixture of beta-D-glucose, L-arabinose, D-xylose, D-galactose, D-maltose, D-mannose and D-cellobiose as substrate (15 mmol/l each)
0.4
-
NAD-GDH, using 10 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.55
-
beta-D-glucose as the sole carbon source and L-arabinose as substrate
0.6
-
beta-D-glucose as the sole carbon source and D-mannose as substrate
0.62
-
beta-D-glucose as the sole carbon source and D-maltose as substrate
0.67
-
NAD-GDH, using 50 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.72
-
NAD-GDH, using 20 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
0.78
-
beta-D-glucose as the sole carbon source and D-xylose as substrate
0.83
-
beta-D-glucose as the sole carbon source and beta-D-glucose as substrate
0.91
-
beta-D-glucose as the sole carbon source and D-galactose as substrate
1.1
-
NAD-GDH, using 30 g/l glucose as excessive carbon source and 0.132 g/l (NH4)SO4
2.25
-
-
3.57
-
-
32
-
purified recombinant enzyme
33.6
-
-
105
-
-
2000
above, purified recombinant catalytic alpha-subunit, 40°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
8.5 - 9
9.9
-
-
10.5
-
activity with D-glucose 6-phosphate and NADP+
10.7
-
cell free extracts
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11
-
50% of maximal activity at pH 4.5 and pH 11.0
6 - 9.5
-
pH 6.0: about 40% of maximal activity, pH 9.5: about 45% of maximal activity
7 - 8.5
-
pH 7.0: 70% of maximal activity with glucose and NAD+ and about 55% of the activity with glucose and NADP+, pH 8.5: about 55% of maximal activity with glucose and NAD+ and about 75% of the activity with glucose and NADP+
7.5 - 10.5
-
at pH 7.5 and 10.0 respectively 75% and 50% activity compared to optimal pH
8
assay at; assay at
8 - 11
-
about 45% of maximal activity at pH 8.0 and pH 11.0
8.5 - 12
-
pH 8.5: about 35% of maximal activity, pH 12.0: about 65% of maximal activity
additional information
-
sharp drop in activity at alkaline pH of wild-type and mutant Q252L activities, not mutant Q252L/E170K
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 48
-
15°C: about 35% of maximal activity, 48°C: 60% of maximal activity
20 - 40
-
20°C: about 70% of maximal activity, 40°C: about 60% of maximal activity
37 - 77
-
37°C: 20% of maximal activity, 77°C: optimum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.05
-
isoelectric focusing, strain 93-1
4.4
-
strain 150-1
4.7 - 4.8
4.9
-
isoelectric focusing
6
-
isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed
7.1
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE