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Information on EC 1.1.1.179 - D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) and Organism(s) Macaca fascicularis and UniProt Accession Q9TQS6

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IUBMB Comments
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming).
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This record set is specific for:
Macaca fascicularis
UNIPROT: Q9TQS6
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The taxonomic range for the selected organisms is: Macaca fascicularis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nadp+-dependent d-xylose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADP+-dependent D-xylose dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,5-lactone-forming)
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming).
CAS REGISTRY NUMBER
COMMENTARY hide
83534-37-6
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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
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
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-
?
additional information
?
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D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
-
-
?
additional information
?
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D-xylose dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyacetophenone
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isoascorbic acid
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 90
D-xylose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 2.6
D-xylose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHDH_MACFA
334
0
36435
Swiss-Prot
Secretory Pathway (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained at 19.9°C in a culture plate via the vapour-diffusion method, crystal structure of dimeric D-xylose dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A36D
site-directed mutagenesis
D280A
by site-directed mutagenesis
F154A
by site-directed mutagenesis
F279A
by site-directed mutagenesis
H76Q
by site-directed mutagenesis
H79Q
by site-directed mutagenesis
K97M
by site-directed mutagenesis
K97R
by site-directed mutagenesis
R37A
site-directed mutagenesis
R37D
site-directed mutagenesis
R41A
by site-directed mutagenesis
R41D
by site-directed mutagenesis
W125Y
by site-directed mutagenesis
W254A
by site-directed mutagenesis
W254Y
by site-directed mutagenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.
Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid
Acta Crystallogr. Sect. D
64
532-542
2008
Macaca fascicularis (Q9TQS6)
Manually annotated by BRENDA team