Information on EC 1.1.1.359 - aldose 1-dehydrogenase [NAD(P)+]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.359
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RECOMMENDED NAME
GeneOntology No.
aldose 1-dehydrogenase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Galactose metabolism
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Metabolic pathways
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Pentose phosphate pathway
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xylose degradation IV
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degradation of pentoses
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Entner Doudoroff pathway
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non-pathway related
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + NADP+ + H2O
?
show the reaction diagram
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?
6-deoxy-D-glucose + NAD+ + H2O
?
show the reaction diagram
6-deoxy-D-glucose + NADP+ + H2O
?
show the reaction diagram
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-
-
-
?
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
show the reaction diagram
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
show the reaction diagram
D-altrose + NADP+ + H2O
?
show the reaction diagram
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-
-
?
D-fucose + NAD+ + H2O
?
show the reaction diagram
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-
-
-
?
D-fucose + NADP+ + H2O
?
show the reaction diagram
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-
-
-
?
D-galactose + NAD+ + H2O
?
show the reaction diagram
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?
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
show the reaction diagram
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
show the reaction diagram
D-xylose + NAD+ + H2O
?
show the reaction diagram
D-xylose + NADP+ + H2O
?
show the reaction diagram
L-arabinose + NAD+ + H2O
?
show the reaction diagram
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?
L-arabinose + NADP+ + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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1 mM, pH 9, 22C, 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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44 - 72.5
beta-D-glucose
0.44 - 204
D-galactose
0.18 - 76.3
D-xylose
0.47 - 0.5
L-arabinose
1.2
NAD+
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pH 9.0, 70C, cosubstrate: beta-D-glucose; pH 9.0, 70C, cosubstrate: D-xylose
0.03 - 0.29
NADP+
additional information
NAD+
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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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 75
beta-D-glucose
7 - 61.3
D-galactose
7 - 81
D-xylose
41
L-arabinose
Sulfolobus solfataricus
Q7LYI9
pH 6.5, 70C, cosubstrate: NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 50
beta-D-glucose
96
0.04 - 108
D-galactose
71
0.11 - 261
D-xylose
115
82
L-arabinose
Sulfolobus solfataricus
Q7LYI9
pH 6.5, 70C, cosubstrate: NAD+
206
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
NADPH
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pH 9.0, 70C, substrate: glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
320
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pH 7.0, 55C
437
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pH 9.0, 70C
458
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pH 8.0, 55C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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assay at, measured at room temperature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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gel filtration in presence of 5% SDS
38000
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4 * 38000
39400
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4 * 39400, SDS-PAGE
40849
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4 * 40849, calculated from sequence
41000
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4 * 41000, SDS-PAGE
60000
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gel filtration in presence of 6 M guanidinium chloride
124000
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gel filtration
130000
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equilibrium-sedimentation
155000
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gel filtration
160000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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
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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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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the enzyme stability does not vary significantly in the pH range 5-9
639110
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
55
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catalytic activity is retained after 9 h
75
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half-life: 3 h
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 hide
LITERATURE
Acetone
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50% (v/v), no appreciable loss of activity
Ethanol
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50% (v/v), no appreciable loss of activity
Ethylene glycol
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preparations became inactivated irreversibly when stored in the absence of ethylene glycol
Methanol
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50% (v/v), no appreciable loss of activity
urea
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4 M, no appreciable loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37C, protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
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4C, 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
expression in Escherichi coli
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expression in Escherichia coli
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expression in Escherichia coli JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T41A
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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
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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