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Information on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+] and Organism(s) Saccharolobus solfataricus and UniProt Accession O93715
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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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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
hexose-6-phosphate dehydrogenase, glcdh-i, glcdh-ii, ssgdh, glcdh-iwg3, bmglcdh-iv, lsgdh, bzgdh, nad(p)-dependent glucose dehydrogenase, hexose phosphate dehydrogenase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-D-glucose:NAD(P)+ 1-oxidoreductase
-
-
-
-
D-glucose dehydrogenase (NAD(P))
-
-
-
-
GDH
-
-
-
-
general stress protein 74
-
-
-
-
GlcDH
-
-
-
-
GSP74
-
-
-
-
hexose phosphate dehydrogenase
-
-
-
-
hexose-6-phosphate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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
9028-53-9
-
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
beta-D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
-
-
?
D-galactose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
equally active compared to beta-D-glucose
-
-
?
D-glucose + 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
-
-
-
?
D-glucose + 1-benzyl-3-carbamoylpyridin-1-ium chloride
D-glucono-1,5-lactone + reduced 1-benzyl-3-carbamoylpyridin-1-ium chloride
-
-
-
?
D-glucose + 1-phenethyl-1,4-dihydropyridine-3-carboxamide
D-glucono-1,5-lactone + reduced 1-phenethyl-1,4-dihydropyridine-3-carboxamide
-
-
-
?
D-xylose + NAD(P)+
D-xylono-1,5-lactone + NAD(P)H + H+
-
-
-
?
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-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 + 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+
-
25% of the activity with D-glucose and NAD+
-
-
?
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(P)+
D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
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-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
26% activity compared to D-glucose
-
-
r
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-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
15% of the activity with D-glucose and NAD+
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
activity with substrate D-galactose in presence of cosubstrate NADP+
-
-
?
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-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
no activity
-
-
?
D-ribose + NADP+
D-ribono-1,5-lactone + NADPH
-
4% of the activity with D-glucose and NADP+
-
-
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
28% of the activity with D-glucose and NAD+
-
-
?
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+
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+
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+
-
-
?
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+
-
-
?
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
-
-
?
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 + H+
first step of the non-phosphorylative Entner-Doudoroff pathway
-
-
ir
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+
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
dual cofactor specificity due to presence of Asn215, His217, and the GXGXXA motif
-
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+
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+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
enzyme contains the catalytic zinc binding residues Cys39 and His66, no increase in activity by addition of 0.1 mM ZnCl2
additional information
not affected by 0.1 mM CaCl2 and MgCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, room temperature, pH 9.0, rapid inactivation
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, room temperature, pH 9.0, 50% inactivation
N-ethylmaleimide
-
3 mM, room temperature, pH 9.0, 50% inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
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
2.64
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
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
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
0.14
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
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
-
0.00008
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00095
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00162
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
0.00283
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T
0.00286
NAD+
pH and temperature not specified in the publication, mutant enzyme I192V
0.00678
NAD+
pH and temperature not specified in the publication, wild-type enzyme
0.00838
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.00006
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.00009
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
0.00011
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.00018
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.00073
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
0.0017
1-(3-phenylpropyl)-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
0.00006
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.00009
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.00011
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.00016
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, wild-type enzyme
-
0.00019
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.00104
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
0.00164
1-benzyl-3-carbamoylpyridin-1-ium chloride
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
0.00004
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306G
-
0.0002
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T
-
0.00024
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, wild-type enzyme
-
0.00029
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192V
-
0.00058
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
-
0.00063
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme V306I
-
0.00517
1-phenethyl-1,4-dihydropyridine-3-carboxamide
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
-
0.00019
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306G
0.00061
NAD+
pH and temperature not specified in the publication, mutant enzyme V306G
0.000974
NAD+
pH and temperature not specified in the publication, mutant enzyme V306I
0.00565
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T/V306I
0.00613
NAD+
pH and temperature not specified in the publication, mutant enzyme I192V
0.00778
NAD+
pH and temperature not specified in the publication, mutant enzyme I192T
0.01594
NAD+
pH and temperature not specified in the publication, wild-type enzyme
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in glucose catabolism via the branched EntnerDoudoroff pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion using a mother liquor of 12% (v/v) polyethylene glycol 4000, 0.1 M MES (pH 5.8), and 3% (v/v) propan-2-ol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I192T
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
I192T/V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 3fold lower than the kcat/Km-value of the wild-type enzyme
I192T/V306I
mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor
V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are slightly higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 2fold lower than the kcat/Km-value of the wild-type enzyme
V306I
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2 M urea, 24 h, room temperature, no loss of activity, slow decrease at 4 M
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration on Superdex 75 26/60, anion exchange chromatography, and affinity chromatography using Reactive Red-500 dye affinity medium and an NaCl gradient of 0 to 1.5 M
native enzyme by gel filtration, recombinant enzyme from Escherichia coli by heat denaturation, and affinity gel chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
enzymatic reduction of the nicotinamide biomimetic cofactors 1-phenethyl-1,4-dihydropyridine-3-carboxamide using glucose dehydrogenase mutant I192T/V306I provides a regeneration system for artificial cofactors. The I192T/V306I mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Lamble, H.J.; Heyer, N.I.; Bull, S.D.; Hough, D.W.; Danson, M.J.
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
J. Biol. Chem.
278
34066-34072
2003
Saccharolobus solfataricus (O93715)
Theodossis, A.; Milburn, C.C.; Heyer, N.I.; Lamble, H.J.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. F
F61
112-115
2005
Saccharolobus solfataricus
Milburn, C.C.; Lamble, H.J.; Theodossis, A.; Bull, S.D.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Biol. Chem.
281
14796-14804
2006
Saccharolobus solfataricus (O93715)
Haferkamp, P.; Kutschki, S.; Treichel, J.; Hemeda, H.; Sewczyk, K.; Hoffmann, D.; Zaparty, M.; Siebers, B.
An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?
Biochem. Soc. Trans.
39
77-81
2011
Saccharolobus solfataricus (Q97U21)
Haferkamp, P.
Biochemical studies of enzymes involved in glycolysis of the thermoacidophilic crenarchaeon Sulfolobus solfataricus
PH. D. Thesis Universitt Duisburg-Essen
2011
0000
2011
Saccharolobus solfataricus (Q97U21), Saccharolobus solfataricus DSM 1617 (Q97U21)
-
Nowak, C.; Pick, A.; Lommes, P.; Sieber, V.
Enzymatic reduction of nicotinamide biomimetic cofactors using an engineered glucose dehydrogenase providing a regeneration system for artificial cofactors
ACS Catal.
7
5202-5208
2017
Saccharolobus solfataricus (O93715)
-
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