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Information on EC 1.1.1.359 - aldose 1-dehydrogenase [NAD(P)+] for references in articles please use BRENDA:EC1.1.1.359Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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aldose 1-dehydrogenase [NAD(P)+]
-
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an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
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-
-
-
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D-xylose degradation IV
-
-
degradation of pentoses
-
-
Entner Doudoroff pathway
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-
Pentose phosphate pathway
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-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
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an aldopyranose:NAD(P)+ 1-oxidoreductase
The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
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Uniprot
brenda
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SwissProt
brenda
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Uniprot
brenda
-
SwissProt
brenda
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physiological function
in glucose catabolism via the branched EntnerDoudoroff pathway the enzyme might acquire important function at higher D-glucose concentrations and in the presence of NAD+. It seems to have additional functions in the catabolism of D-galactose via the same pathway as well as in degradation pathways of D-xylose and L-arabinose
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2-deoxy-D-glucose + NADP+ + H2O
?
-
-
-
?
6-deoxy-D-glucose + NAD+ + H2O
?
6-deoxy-D-glucose + NADP+ + H2O
?
-
-
-
-
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
D-altrose + NADP+ + H2O
?
-
-
-
?
D-fucose + NAD+ + H2O
?
-
-
-
-
?
D-fucose + NADP+ + H2O
?
-
-
-
-
?
D-galactose + NAD+ + H2O
?
-
-
-
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
L-arabinose + NAD+ + H2O
?
-
-
-
-
?
L-arabinose + NADP+ + H2O
?
additional information
?
-
6-deoxy-D-glucose + NAD+ + H2O
?
-
-
-
?
6-deoxy-D-glucose + NAD+ + H2O
?
-
-
-
-
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
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kcat/Km for beta-D-glucose in the reaction with NAD+ is 1.4fold higher than the kcat/Km value for beta-D-glucose in the reaction with NADP+
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-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
when NAD+ serves as electron acceptor, D-glucose is oxidized at the highest rate among the substrates tested. No reverse reaction is evident, under various reaction conditions, when gluconic acid is used as substrate
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
it is likely that the first product of this reaction is delta-gluconolactone, which is readily converted into the acid. The lactone hydrolysis is facilitated by the high temperature and the slight alkaline pH value of the standard reaction conditions, thus explaining why no reverse reaction is observed under these conditions when delta-gluconolactone is used as substrate. A very slow NADH-dependent reduction of delta-gluconolactone by glucose dehydrogenase is observed at pH 7.0 and 37°C
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-
?
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
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kcat/Km for beta-D-glucose in the reaction with NADP+ is 1.4fold lower than the kcat/Km value for beta-D-glucose in the reaction with NAD+
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
-
?
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
ir
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
-
-
-
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
the activity is 70% of the activity with beta-D-glucose + NADP+
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-
?
D-xylose + NAD+ + H2O
?
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-
-
?
D-xylose + NAD+ + H2O
?
-
-
-
-
?
D-xylose + NAD+ + H2O
?
-
-
-
?
D-xylose + NADP+ + H2O
?
-
-
-
?
D-xylose + NADP+ + H2O
?
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-
-
-
?
D-xylose + NADP+ + H2O
?
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-
-
?
D-xylose + NADP+ + H2O
?
-
-
-
?
L-arabinose + NADP+ + H2O
?
-
-
-
-
?
L-arabinose + NADP+ + H2O
?
no activity with NAD+
-
-
?
L-arabinose + NADP+ + H2O
?
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-
-
?
additional information
?
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the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
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-
-
additional information
?
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no activity with mannose or glucose 6-phosphate
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additional information
?
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Q7LYI9
the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
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-
-
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NAD+
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the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
NAD+
-
when NAD+ serves as electron acceptor, D-glucose is oxidized at the highest rate among the substrates tested
NAD+
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kcat/Km for beta-D-glucose in the reaction with NAD+ is 1.4fold higher than the kcat/Km value for beta-D-glucose in the reaction with NADP+
NADP+
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the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
NADP+
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by using NADP+ as coenzyme D-xylose and 2-deoxy-D-glucose are oxidized at the highest rate
NADP+
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kcat/Km for beta-D-glucose in the reaction with NADP+ is 1.4fold lower than the kcat/Km value for beta-D-glucose in the reaction with NAD+
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Ca2+
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20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mg2+
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20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mn2+
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20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Zinc
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the enzyme possess the catalytic zinc binding residues Cys-39 and His-66
additional information
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Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
additional information
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no significant increase in the presence of ZnCl2, CaCl2, or MgCl2, at final concentrations of 0.1 mM
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2-mercaptoethanol
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1 mM, pH 9, 22°C, rapid inactivation
5,5'-dithiobis-(2-nitrobenzoic acid)
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1 mM, 50% inactivation
acetone
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40% (v/v), 40% activity
ethanol
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40% (v/v), 30% activity
methanol
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40% (v/v), 50% activity
NADPH
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inhibits the NAD+-dependentcarbohydrate oxidations in a competitive manner with respect to NAD+
NEM
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3 mM, 2 h, 50% inactivation
Urea
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40% (v/v), 85% activity
additional information
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galactose (0.04 mM), mannose (0.04 mM) and ribose (0.04 mM) do not inhibit glucose oxidation by NAD+
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EDTA
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50 mM, 95% inhibition
EDTA
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10 mM, 60% loss of activity
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0.44 - 72.5
beta-D-glucose
1.2
NAD+
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pH 9.0, 70°C, cosubstrate: beta-D-glucose; pH 9.0, 70°C, cosubstrate: D-xylose
additional information
NAD+
-
Km is superior to 30 mM. The Km value for NAD+ can not be defined precisely as it is impossible to reach saturation of the enzyme
0.44
beta-D-glucose
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pH 9.0, 70°C, cosubstrate: NADP+
1.3
beta-D-glucose
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pH 7.5, 70°C, cofactor: NADP+
1.3
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
1.3
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
1.5
beta-D-glucose
-
pH 7.5, 70°C, cofactor: NAD+
1.5
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
1.5
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
8
beta-D-glucose
-
pH 9.0, 70°C, cosubstrate: NAD+
9.4
beta-D-glucose
-
pH 8.0, 55°C
10
beta-D-glucose
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pH 7.0, 55°C
24.8
beta-D-glucose
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pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
33.3
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
59
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
72.5
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.44
D-galactose
-
pH 7.5, 70°C, cofactor: NADP+
0.44
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
0.44
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
0.57
D-galactose
-
pH 7.5, 70°C, cofactor: NAD+
0.57
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
0.57
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
22
D-galactose
-
pH 9.0, 70°C, cosubstrate: NADP+
109
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
118
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
175
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
204
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.18
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
0.18
D-xylose
-
pH 8.0, 70°C, native enzyme from xylose-grown cell extract; pH 8.0, 70°C, recombinant enzyme
0.18
D-xylose
pH 6.5, 70°C, cosubstrate: NADP+
0.25
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
0.25
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
2.2
D-xylose
-
pH 9.0, 70°C, cosubstrate: NADP+
20.4
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
29.2
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
65.8
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
68
D-xylose
-
pH 9.0, 70°C, cosubstrate: NAD+
76.3
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.47
L-arabinose
-
pH 8.0, 70°C, native enzyme from xylose-grown cell extract
0.5
L-arabinose
-
pH 8.0, 70°C, recombinant enzyme
0.5
L-arabinose
pH 6.5, 70°C, cosubstrate: NAD+
0.03
NADP+
-
pH 9.0, 70°C, cosubstrate: beta-D-glucose; pH 9.0, 70°C, cosubstrate: D-galactose; pH 9.0, 70°C, cosubstrate: D-xylose
0.113
NADP+
-
pH 7.0, 55°C
0.29
NADP+
-
pH 8.0, 55°C
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41
L-arabinose
pH 6.5, 70°C, cosubstrate: NAD+
4
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
6
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
14
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
39
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
47.7
beta-D-glucose
-
pH 7.5, 70°C, cofactor: NADP+
47.7
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
48
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
74.9
beta-D-glucose
-
pH 7.5, 70°C, cofactor: NAD+
74.9
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
75
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
7
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
8
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
22
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
37
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
37
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
37.4
D-galactose
-
pH 7.5, 70°C, cofactor: NADP+
56
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
61
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
61
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
61.3
D-galactose
-
pH 7.5, 70°C, cofactor: NAD+
7
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
12
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
22
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
44
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
47
D-xylose
pH 6.5, 70°C, cosubstrate: NADP+
61
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
61
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
81
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
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82
L-arabinose
pH 6.5, 70°C, cosubstrate: NAD+
0.07
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.09
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.4
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
1.6
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
36.7
beta-D-glucose
-
pH 7.5, 70°C, cofactor: NADP+
36.7
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
37
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
49.9
beta-D-glucose
-
pH 7.5, 70°C, cofactor: NAD+
49.9
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
50
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
0.04
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V; pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.2
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
0.5
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
85
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
85
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
85.1
D-galactose
-
pH 7.5, 70°C, cofactor: NADP+
107
D-galactose
-
pH 7.5, 70°C, cofactor: NAD+
108
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
108
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
0.11
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.15
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
1.1
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
2.8
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
245
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
245
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
246
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
261
D-xylose
pH 6.5, 70°C, cosubstrate: NADP+
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0.075
NADPH
-
pH 9.0, 70°C, substrate: glucose
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9
-
assay at, measured at room temperature
8
-
-
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70
-
assay at
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-
-
brenda
-
-
-
brenda
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30000
-
gel filtration in presence of 5% SDS
39400
-
4 * 39400, SDS-PAGE
40849
-
4 * 40849, calculated from sequence
41000
-
4 * 41000, SDS-PAGE
60000
-
gel filtration in presence of 6 M guanidinium chloride
130000
-
equilibrium-sedimentation
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tetramer
-
4 * 40849, calculated from sequence; 4 * 41000, SDS-PAGE
tetramer
-
4 * 39400, SDS-PAGE
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hanging drop, vapor-diffusion method, crystal structure of the apo form of glucose dehydrogenase to a resolution of 1.8 A and a complex with its required cofactor, NADP+, to a resolution of 2.3 A. Complexes of the enzyme with D-glucose and D-xylose are presented to resolutions of 1.6 and 1.5 A. A T41A mutation is engineered to enable the trapping of substrate in the crystal
-
the best crystals to date diffract to 1.8 A on a synchrotron source, have orthorhombic symmetry and belong to space group P2(1)2(1)2
-
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5 - 9
-
the enzyme stability does not vary significantly in the pH range 5-9
639110
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37
-
protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
55
-
catalytic activity is retained after 9 h
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dehydrogenase preparations became inactivated irreversibly when stored in the absence of ethylene glycol and Mg2+, at very low protein concentration, or during freezing and thawing
-
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Acetone
-
50% (v/v), no appreciable loss of activity
Ethanol
-
50% (v/v), no appreciable loss of activity
Ethylene glycol
-
preparations became inactivated irreversibly when stored in the absence of ethylene glycol
Methanol
-
50% (v/v), no appreciable loss of activity
urea
-
4 M, no appreciable loss of activity
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37°C, protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
-
4°C, 20 mM MgCl2 and 20% (v/v) ethylene glycol, stable for several months
-
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enzyme from Sulfolobus solfataricus cell extract and recombinant enzyme expressed in Escherichia coli
-
-
-
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expression in Escherichi coli
-
expression in Escherichia coli
-
expression in Escherichia coli JM109
-
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T41A
-
kcat/Km value of the mutant enzyme for beta-D-glucose (with NAD+) is about 30fold lower compared to wild-type enzyme, kcat/Km value of the mutant enzyme for beta-D-flucose (with NADP+) is about 90fold lower compared to wild-type enzyme
T41V
-
kcat/Km value of the mutant enzyme for beta-D-glucose (with NAD+) is about 555fold lower compared to wild-type enzyme, kcat/Km value of the mutant enzyme for beta-D-flucose (with NADP+) is about 530fold lower compared to wild-type enzyme
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GLCDH_SULSF
366
40891
Swiss-Prot
GLCD1_SULSO
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
366
40891
Swiss-Prot
GLCDH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
361
40250
Swiss-Prot
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Smith, L.D.; Budgen, N.; Bungard, S.J.; Danson, M.J.; Hough, D.W.
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
Biochem. J.
261
973-977
1989
Thermoplasma acidophilum (P13203)
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
Sulfolobus solfataricus (O93715)
brenda
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
Sulfolobus solfataricus (O93715)
brenda
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
Sulfolobus solfataricus (O93715)
brenda
Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.
Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius
J. Biol. Chem.
285
33701-33709
2010
Sulfolobus solfataricus (O93715), Sulfolobus solfataricus P2 (O93715)
brenda
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
61
112-115
2005
Sulfolobus solfataricus (O93715)
brenda
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
Sulfolobus solfataricus (Q7LYI9)
brenda
Bright, J.R.; Byrom, D.; Danson, M.J.; Hough, D.W.; Towner, P.
Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum
Eur. J. Biochem.
211
549-554
1993
Thermoplasma acidophilum (P13203)
brenda
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