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Information on EC 1.1.1.359 - aldose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.359
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.359 aldose 1-dehydrogenase [NAD(P)+]
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 enzyme appears in viruses and cellular organisms
showSynonyms
gdh-1, glucose dehydrogenase, SsGDH, SSO3003, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
D-xylose degradation IV
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + NADP+ + H2O
?
Substrates: -
Products: -
Products: -
?
6-deoxy-D-glucose + NAD+ + H2O
?
Substrates: -
Products: -
Products: -
?
6-deoxy-D-glucose + NADP+ + H2O
?
Substrates: -
Products: -
Products: -
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: 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+
Products: -
Products: -
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: 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
Products: -
Products: -
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: 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+
Products: -
Products: -
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: 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
Products: -
Products: -
?
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
Substrates: the activity is 70% of the activity with beta-D-glucose + NADP+
Products: -
Products: -
?
D-xylose + NAD+ + H2O
?
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+ + H2O
?
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+ + H2O
?
Substrates: no activity with NAD+
Products: -
Products: -
?
L-arabinose + NADP+ + H2O
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with mannose or glucose 6-phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the enzyme iss involved in aldose catabolism via the branched variant of the EntnerDoudoroff pathway
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
NAD+
the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
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+
NADP+
by using NADP+ as coenzyme D-xylose and 2-deoxy-D-glucose are oxidized at the highest rate
NADP+
the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
no significant increase in the presence of ZnCl2, CaCl2, or MgCl2, at final concentrations of 0.1 mM
additional information
Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoic acid)
1 mM, 50% inactivation
NADPH
inhibits the NAD+-dependentcarbohydrate oxidations in a competitive manner with respect to NAD+
additional information
galactose (0.04 mM), mannose (0.04 mM) and ribose (0.04 mM) do not inhibit glucose oxidation by NAD+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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, cosubstrate: NAD+, wild-type enzyme
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, cosubstrate: NADP+, wild-type enzyme
0.57
D-galactose
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
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
0.25
D-xylose
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
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
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
48
beta-D-glucose
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
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
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
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
37
beta-D-glucose
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
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
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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). GLCDH_SACSO
366
0
40891
Swiss-Prot
other Location (Reliability: 4)
GLCDH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
361
0
40250
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLCD1_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
366
0
40891
Swiss-Prot
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
gel filtration in presence of 6 M guanidinium chloride
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
the enzyme stability does not vary significantly in the pH range 5-9
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethylene glycol
preparations became inactivated irreversibly when stored in the absence of ethylene glycol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme from Sulfolobus solfataricus cell extract and recombinant enzyme expressed in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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 (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
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
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.359)
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