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EC Tree
IUBMB Comments 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.
The taxonomic range for the selected organisms is: Saccharolobus solfataricus The enzyme appears in selected viruses and cellular organisms
Synonyms
gdh-1, glucose dehydrogenase, SsGDH,
SSO3003 ,
more
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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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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+
-
-
-
?
D-xylose + NAD+ + H2O
?
-
-
-
?
D-xylose + NADP+ + H2O
?
-
-
-
?
L-arabinose + NAD+ + H2O
?
-
-
-
?
L-arabinose + NADP+ + H2O
?
-
-
-
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
ir
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
?
D-xylose + NAD+ + H2O
?
-
-
-
?
D-xylose + NADP+ + H2O
?
-
-
-
?
L-arabinose + NADP+ + H2O
?
no activity with NAD+
-
-
?
additional information
?
-
the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
-
-
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
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+
-
-
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 + 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
-
-
?
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
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
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additional information
?
-
the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
-
-
?
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NAD+
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+
NAD+
when NAD+ serves as electron acceptor, D-glucose is oxidized at the highest rate among the substrates tested
NADP+
-
NADP+
by using NADP+ as coenzyme D-xylose and 2-deoxy-D-glucose are oxidized at the highest rate
NADP+
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+
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mg2+
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mn2+
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Zinc
the enzyme possess the catalytic zinc binding residues Cys-39 and His-66
additional information
Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
additional information
no significant increase in the presence of ZnCl2, CaCl2, or MgCl2, at final concentrations of 0.1 mM
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2-mercaptoethanol
1 mM, pH 9, 22°C, rapid inactivation
5,5'-dithiobis-(2-nitrobenzoic acid)
1 mM, 50% inactivation
NADPH
inhibits the NAD+-dependentcarbohydrate oxidations in a competitive manner with respect to NAD+
NEM
3 mM, 2 h, 50% inactivation
additional information
galactose (0.04 mM), mannose (0.04 mM) and ribose (0.04 mM) do not inhibit glucose oxidation by NAD+
-
EDTA
50 mM, 95% inhibition
EDTA
10 mM, 60% loss of activity
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0.44 - 72.5
beta-D-glucose
0.5
L-arabinose
pH 6.5, 70°C, cosubstrate: NAD+
0.44
beta-D-glucose
pH 9.0, 70°C, cosubstrate: NADP+
1.3
beta-D-glucose
pH 7.5, 70°C, cofactor: NADP+
1.3
beta-D-glucose
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
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
8
beta-D-glucose
pH 9.0, 70°C, cosubstrate: NAD+
24.8
beta-D-glucose
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
0.57
D-galactose
pH 7.5, 70°C, cofactor: NAD+
0.57
D-galactose
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
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 8.0, 70°C, recombinant enzyme
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
0.25
D-xylose
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
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
1.2
NAD+
pH 9.0, 70°C, cosubstrate: beta-D-glucose
1.2
NAD+
pH 9.0, 70°C, cosubstrate: D-xylose
0.03
NADP+
pH 9.0, 70°C, cosubstrate: beta-D-glucose
0.03
NADP+
pH 9.0, 70°C, cosubstrate: D-galactose
0.03
NADP+
pH 9.0, 70°C, cosubstrate: D-xylose
1.3
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
1.5
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
0.44
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
0.57
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
0.18
D-xylose
pH 6.5, 70°C, cosubstrate: NADP+
0.25
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
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47.7 - 74.9
beta-D-glucose
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+
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+
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
37.4
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
61.3
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
61
D-xylose
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
81
D-xylose
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
47.7
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
74.9
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
37
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
61
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
47
D-xylose
pH 6.5, 70°C, cosubstrate: NADP+
61
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
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36.7 - 49.9
beta-D-glucose
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+
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+
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
0.04
D-galactose
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
85.1
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
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
246
D-xylose
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
36.7
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NADP+
49.9
beta-D-glucose
pH 6.5, 70°C, cosubstrate: NAD+
85
D-galactose
pH 6.5, 70°C, cosubstrate: NADP+
108
D-galactose
pH 6.5, 70°C, cosubstrate: NAD+
245
D-xylose
pH 6.5, 70°C, cosubstrate: NAD+
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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9
assay at, measured at room temperature
8
-
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-
Uniprot
brenda
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-
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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GLCDH_SACSO
366
0
40891
Swiss-Prot
-
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130000
equilibrium-sedimentation
30000
gel filtration in presence of 5% SDS
40849
4 * 40849, calculated from sequence
41000
4 * 41000, SDS-PAGE
60000
gel filtration in presence of 6 M guanidinium chloride
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tetramer
4 * 41000, SDS-PAGE
tetramer
4 * 40849, calculated from sequence
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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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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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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
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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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Ethylene glycol
preparations became inactivated irreversibly when stored in the absence of ethylene glycol
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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 Escherichia coli
expression in Escherichia coli JM109
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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 (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
Saccharolobus 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
Saccharolobus 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
Saccharolobus solfataricus (O93715), Saccharolobus 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
Saccharolobus 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
Saccharolobus solfataricus (Q7LYI9)
brenda