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

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The enzyme appears in viruses and cellular organisms

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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
D-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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Pentose phosphate pathway
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Galactose metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in glucose catabolism via the branched Entner–Doudoroff 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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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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-
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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 Entner–Doudoroff pathway
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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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, 70°C, cosubstrate: beta-D-glucose; pH 9.0, 70°C, 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
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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
pH 6.5, 70°C, cosubstrate: NAD+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 50
beta-D-glucose
0.04 - 108
D-galactose
0.11 - 261
D-xylose
82
L-arabinose
pH 6.5, 70°C, cosubstrate: NAD+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
NADPH
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pH 9.0, 70°C, substrate: glucose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
320
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pH 7.0, 55°C
437
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pH 9.0, 70°C
458
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pH 8.0, 55°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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assay at, measured at room temperature
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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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
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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 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
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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
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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
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.359)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)