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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glucose dehydrogenase, d-aldohexose dehydrogenase,
more
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D-aldohexose dehydrogenase
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D-glucose:NAD oxidoreductase
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dehydrogenase, glucose (nicotinamide adenine dinucleotide)
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GDH
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glucose dehydrogenase
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glucose dehydrogenase
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glucose dehydrogenase
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-
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D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+
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D-glucose:NAD+ 1-oxidoreductase
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2-amino-2-deoxy-D-glucose + NAD+
? + NADH
-
26% activity compared to D-glucose in combination with NAD+
-
?
2-amino-2-deoxy-D-glucose + NADP+
? + NADPH
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5% activity compared to D-glucose in combination with NAD+
-
?
2-deoxy-D-galactose + NAD+
2-deoxy-D-galactono-1,5-lactone + NADH
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
2-deoxy-D-glucose + NADP+
? + NADPH
-
25% activity compared to D-glucose in combination with NAD+
-
?
3,6-dideoxy-D-galactose + NAD+
3,6-dideoxy-D-galactono-1,5-lactone + NADH
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-
-
?
6-deoxy-D-galactose + NAD+
6-deoxy-D-galactono-1,5-lactone + NADH
-
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
6-deoxy-D-glucose + NADP+
? + NADPH
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9% activity compared to D-glucose in combination with NAD+
-
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
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-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
-
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH + H+
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5% activity compared to D-glucose in combination with NAD+
-
?
D-altrose + NADP+
? + NADPH
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12% activity compared to D-glucose in combination with NAD+
-
?
D-fucose + NAD+
D-fucono-1,5-lactone + NADH + H+
-
-
-
r
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
D-galactose + NADH
D-galactono-1,5-lactone + NADH + H+
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15% activity compared to D-glucose in combination with NAD+
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
D-gulose + NAD+
? + NADH
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8% activity compared to D-glucose in combination with NAD+
-
?
D-gulose + NADP+
? + NADPH
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12% activity compared to D-glucose in combination with NAD+
-
?
D-idose + NAD+
? + NADH
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65% activity compared to D-glucose in combination with NAD+
-
?
D-idose + NADP+
? + NADPH
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12% activity compared to D-glucose in combination with NAD+
-
?
D-mannose + NAD+
D-manno-1,5-lactone + NADH
D-mannose + NADP+
? + NADPH
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4% activity compared to D-glucose in combination with NAD+
-
?
D-ribose + NADP+
? + NADPH
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4% activity compared to D-glucose in combination with NAD+
-
?
D-xylose + NAD+
? + NADH
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26% activity compared to D-glucose in combination with NAD+
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?
D-xylose + NADP+
? + NADPH
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28% activity compared to D-glucose in combination with NAD+
-
?
additional information
?
-
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+
-
12% activity compared to D-glucose in combination with NAD+
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
12% activity compared to D-glucose in combination with NAD+
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
66% activity compared to D-glucose in combination with NAD+
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
66% activity compared to D-glucose in combination with NAD+
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
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-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
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-
-
?
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 + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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100% activity
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?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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100% activity
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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9% activity compared to D-glucose in combination with NAD+
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?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
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9% activity compared to D-glucose in combination with NAD+
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?
D-mannose + NAD+
D-manno-1,5-lactone + NADH
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?
D-mannose + NAD+
D-manno-1,5-lactone + NADH
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?
additional information
?
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no activity with: D-glucuronic acid, D-galacturonic acid, D-galactose 6-phosphate, D-glucose 6-phosphate, D-glucosamine, N-acetyl-D-glucosamine, 6-deoxy-D-allose, 6-iodo-6-deoxy-D-galactose, 2-acetamide-6-deoxy-D-allose, 2-acetamido-6-deoxy-D-altrose
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?
additional information
?
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no activity with: D-glucuronic acid, D-galacturonic acid, D-galactose 6-phosphate, D-glucose 6-phosphate, D-glucosamine, N-acetyl-D-glucosamine, 6-deoxy-D-allose, 6-iodo-6-deoxy-D-galactose, 2-acetamide-6-deoxy-D-allose, 2-acetamido-6-deoxy-D-altrose
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?
additional information
?
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no activity towards D-mannose,D-galactose, and D-ribose in combination with NAD+
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?
additional information
?
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no activity towards D-mannose,D-galactose, and D-ribose in combination with NAD+
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?
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D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
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?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
-
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?
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NAD+
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-
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Ca2+
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maximally active at 20 mM
Mg2+
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maximally active at 20 mM
Mn2+
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maximally active at 20 mM
additional information
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Zn2+ is partially effective, whereas Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
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2-mercaptoethanol
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rapid inactivation at 1 mM
5,5'-dithiobis-(2-nitrobenzoic acid)
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EDTA
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5% residual activity at 50 mM, addition of Mg2+ in excess restored the initial activity
Guanidinium chloride
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rapid inactivation at 4 M
NADPH
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inhibits the NAD+-dependent carbohydrate oxidations in a competitive manner with respect to NAD+
additional information
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D-alactose, D-mannose and D-ribose, in concentrations as high as 0.04 mM do not inhibit glucose oxidation by NAD+
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22
D-galactose
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in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.44
D-glucose
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in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
8
D-glucose
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in the presence of NAD+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
2.2
D-xylose
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in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
68
D-xylose
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in the presence of NAD+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
1.2
NAD+
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in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
1.2
NAD+
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in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.03
NADP+
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in the presence of D-galactose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.03
NADP+
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in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.03
NADP+
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in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
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0.075
NADPH
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using D-glucose as a substrate
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3
5,5'-dithiobis-(2-nitrobenzoic acid)
Saccharolobus solfataricus
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at 25°C and pH 9
1
N-ethylmaleimide
Saccharolobus solfataricus
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at 25°C and pH 9
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0.7
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unpurified enzyme, at 70°C
437
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after 623fold purification, at 70°C
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8 - 8.5
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Tris-HCl buffer
9 - 10
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glycine-NaOH buffer
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brenda
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brenda
No. 93-1
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brenda
No. 93-1
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brenda
i.e. Acetobacter xylinum
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brenda
IAM 12014
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brenda
IAM 12014
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brenda
MSU-1
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brenda
-
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brenda
-
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brenda
-
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brenda
MSU-1
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brenda
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Q9HK51_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
255
0
27873
TrEMBL
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Q97CM7_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
261
0
28195
TrEMBL
-
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Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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30000
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x * 30000, SDS-PAGE
30100
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
60200
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
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?
-
x * 30000, SDS-PAGE
homodimer
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2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
homodimer
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2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
homotetramer
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4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
homotetramer
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
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E170K
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has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65°C. Stability dependence on salt concentration
E170K/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
P45A/F155Y/V227A
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has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65°C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
E170K
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has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65°C. Stability dependence on salt concentration
E170K/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
P45A/F155Y/V227A
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has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65°C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
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5 - 9
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the enzyme stability does not vary significantly in the pH range 5-9
639110
6 - 8
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30°C, 30 min, stable
285777
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35
-
pH 7.0, 10 min, stable up to
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SDS
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a slow time-dependent decrease of activity is observed in the presence of 0.1% SDS
Acetone
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stable in the presence of chaotropic agents and water-miscible organic solvents such as acetone
Acetone
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stable in the presence of chaotropic agents and water-miscible organic solvents such as acetone
Ethanol
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a slow time-dependent decrease of activity is observed in the presence of ethanol
Ethanol
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a slow time-dependent decrease of activity is observed in the presence of ethanol
Methanol
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stable in the presence of chaotropic agents and water-miscible organic solvents such as methanol
Methanol
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stable in the presence of chaotropic agents and water-miscible organic solvents such as methanol
urea
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a slow time-dependent decrease of activity is observed in the presence of 4 M urea
urea
-
a slow time-dependent decrease of activity is observed in the presence of 4 M urea
additional information
-
2 M urea and 0.05% (w/v) SDS do not cause any loss of enzymic activity
additional information
-
2 M urea and 0.05% (w/v) SDS do not cause any loss of enzymic activity
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37°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 40 days, 50% loss of activity
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4°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, several months, remains stable
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70°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 45 h, 50% loss of activity
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stable to freezing for at least 6 months, pH 7.0, 10 mM sodium phosphate buffer
-
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SP-Sephadex C-50 gel filtration, phenyl-Sepharose column chromatography, and Affi-Gel Blue matrix gel filtration
-
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His-tag GDH variants, into pET28a and expressed in Escherichia coli BL21(DE3)
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biotechnology
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immobilization of GDH1 on the surface of a graphite felt electrode, construction and optimization of an electrochemical bioreactor, co-immobilization of 3,4-dihydroxybenzaldehyde as mediator allows the system to operate at 0.2 V and increases both the activity (2.4-times) and the stability of the immobilized enzyme by 2.2-times, the immobilized enzyme is termed IMGDH1
synthesis
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glucose dehydrogenase and L-carnitine dehydrogenase are coimmobilized in a nanofiltration membrane bioreactor for the continuous production of 1-carnitine from 3-dehydrocarnitine with NADH regeneration
synthesis
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glucose dehydrogenase and L-carnitine dehydrogenase are coimmobilized in a nanofiltration membrane bioreactor for the continuous production of 1-carnitine from 3-dehydrocarnitine with NADH regeneration
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Hu, A.S.L.; Cline, A.L.
The regulation of some sugar dehydrogenases in a Pseudomonad
Biochim. Biophys. Acta
93
237-245
1964
Pseudomonas sp.
brenda
Kobayashi, Y.; Horikoshi, K.
Identification and growth characteristics of alkalophilic Corynebacterium sp. which produces NAD(P)-dependent maltose dehydrogenase and glucose dehydrogenase
Agric. Biol. Chem.
44
41-47
1980
Corynebacterium sp., Corynebacterium sp. No. 93-1
-
brenda
Anderson, R.L.; Dahms, A.S.
D-Aldohexose dehydrogenase
Methods Enzymol.
41
147-150
1975
Pseudomonas sp., Pseudomonas sp. MSU-1
brenda
Lin, S.S.; Miyawaki, O.; Nakamura, K.
Continuous production of L-carnitine with NADH regeneration by a nanofiltration membrane reactor with coimmobilized L-carnitine dehydrogenase and glucose dehydrogenase
J. Biosci. Bioeng.
87
361-364
1999
Pseudomonas putida, Pseudomonas putida IAM 12014
brenda
Giardina, P.; DeBasia, M.G.; DeRosa, M.; Gambacort, A.; Buonocore, V.
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
Biochem. J.
239
517-522
1986
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
brenda
Manjon, A.; Obon, J.M.; Casanova, P.; Fernandez, V.M.; Ilborra1, J.L.
Increased activity of glucose dehydrogenase co-immobilized with a redox mediator in a bioreactor with electrochemical NAD+ regeneration
Biotechnol. Lett.
24
1227-1232
2002
Komagataeibacter xylinus
-
brenda
Vazquez-Figueroa, E.; Yeh, V.; Broering, J.; Chaparro-Riggers, J.; Bommarius, A.
Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media
Protein Eng. Des. Sel.
21
673-680
2008
Bacillus subtilis, Bacillus subtilis 168
brenda
Zhang, X.; Rao, Z.; Zhang, L.; Xu, M.; Yang, T.
Efficient 9alpha-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9alpha-hydroxylase and B. subtilis glucose 1-dehydrogenase with NADH regeneration
SpringerPlus
5
1207
2016
Bacillus subtilis, Bacillus subtilis 168
brenda
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