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Information on EC 1.1.1.179 - D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming)
for references in articles please use BRENDA:EC1.1.1.179
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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
1.1.1.179 D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming)
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).
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
showSynonyms
nadp+-dependent d-xylose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase
-
-
ambiguous
-
D-xylose 1-dehydrogenase (NADP)
-
-
ambiguous
-
D-xylose dehydrogenase
D-xylose-NADP dehydrogenase
-
-
ambiguous
-
D-xylose:NADP+ oxidoreductase
-
-
ambiguous
-
NADP+-dependent D-xylose dehydrogenase
XDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH + H+
also acts, more slowly, on L-arabinose and D-ribose
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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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).
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CAS REGISTRY NUMBER
COMMENTARY
83534-37-6
-
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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
camphorquinone + NADPH
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: 44% of the activity with D-xylose
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
A8BT09
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-gluconolactone + NAD(P)H
Substrates: -
Products: -
Products: -
?
D-glucose + NAD(P)+
D-gluconolactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 20% of the activity with D-xylose
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
Substrates: 20% of the activity with D-xylose
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
A8BT09
Substrates: -
Products: -
Products: -
?
D-glucose + NADP+
D-gluconolactone + NADPH + H+
Substrates: reaction is catalyzed with 70fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
Products: -
Products: -
?
D-glucose + NADP+
D-gluconolactone + NADPH + H+
-
Substrates: reaction is catalyzed with 70fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-mannose + NADP+
D-mannono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-ribose + NADP+
D-ribonolactone + NADPH + H+
Substrates: reaction is catalyzed with 1.8fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
Products: -
Products: -
?
D-ribose + NADP+
D-ribonolactone + NADPH + H+
-
Substrates: reaction is catalyzed with 1.8fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
Products: -
Products: -
?
D-xylose + NAD(P)+
D-xylonolactone + NAD(P)H
Substrates: is highly specific for D-xylose
Products: -
Products: -
?
D-xylose + NAD(P)+
D-xylonolactone + NAD(P)H
-
Substrates: is highly specific for D-xylose
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
Substrates: -
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NAD+
D-xylono-1,5-lactone + NADH + H+
-
Substrates: very low activity compared to NADP+
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
Substrates: Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
Products: -
Products: -
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
-
Substrates: Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
A8BT09
Substrates: best substrate
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
Substrates: Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
Substrates: Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH
A8BT09
Substrates: -
Products: -
Products: -
?
trans-benzene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-benzene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-benzene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-benzene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NADP+
?
-
Substrates: dihydrodiol dehydrogenase activity, probably identical with EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-arabinose, D-ribose, D-glucose and D-galactose are oxidized at 10-30% the rate of D-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols, probably identical with dimeric dihydrodiol dehydrogenase EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-arabinose, D-ribose, D-glucose and D-galactose are oxidized at 10-30% the rate of D-xylose
Products: -
Products: -
?
additional information
?
-
Substrates: no significant oxidation with L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
Products: -
Products: -
?
additional information
?
-
Substrates: no significant oxidation with L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no significant oxidation with L-arabinose, D-arabinose, D-ribose, D-mannose, and L-mannose
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols, probably identical with dimeric dihydrodiol dehydrogenase EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols, probably identical with dimeric dihydrodiol dehydrogenase EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols, probably identical with dimeric dihydrodiol dehydrogenase EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: D-arabinose, D-glucose, D-mannose, D-galactose
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols, probably identical with dimeric dihydrodiol dehydrogenase EC 1.3.1.20
Products: -
Products: -
?
additional information
?
-
-
Substrates: at concentrations of up to 50 mM of L-xylose, D-ribose, D-arabinose, L-arabinose, D-glucose, D-galactose or D-fructose, the enzyme produces little NADPH and the specific activity toward these substrates are below 5% of the activity recorded with D-xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-arabinose, D-ribose, D-glucose and D-galactose are oxidized at 10-30% the rate of D-xylose
Products: -
Products: -
?
additional information
?
-
A8BT09
Substrates: no or poor activity with D-arabinose, D-mannose, L-rhamnose, D-lyxose, D-fructose, D-glyceraldehyde, and DL-glyceraldehyde
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
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: 44% of the activity with D-xylose
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: enzyme has dehydrogenase and reductase activities, enzyme is identical to dihydrodiol dehydrogenase
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
A8BT09
Substrates: best substrate
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
Substrates: initial step in xylose degradation
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
Substrates: initial step in xylose degradation
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
preferred electron acceptor. Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
2.9
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
3.4
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
4.4
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
8 - 9
D-xylose
oxidation reaction of mutant F279A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
11
D-xylose
oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
14
D-xylose
oxidation reaction of mutant W254Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
15
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
36
D-xylose
oxidation reaction of mutant F154A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
41
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
65
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
67
D-xylose
oxidation reaction of mutant W125Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
90
D-xylose
oxidation reaction of mutant W254A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose
additional information
additional information
-
phosphate buffer increases the Km-value, especially for mutant H79Q, compared with Tris buffer
-
additional information
additional information
A8BT09
kinetics, recombinant enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
D-xylose
oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
0.45
D-xylose
oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
0.5
D-xylose
oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
0.9
D-xylose
oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
1
D-xylose
oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
1.2
D-xylose
oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
1.7
D-xylose
oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
2.6
D-xylose
oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
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
10
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
activity increases exponentially with temperature between 25°C and 45°C. 50°C: optimum
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Trichoderma reesei, strain VTT-D-80133, gene xyd1
A8BT09
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (5931 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H79Q
Y180F
additional information
H79Q
-
increase in Km more than 25fold, increase in Kd more than 7fold, with high ionic strength Km increased by 190fold and inhibited the enzyme
additional information
in-frame deletion mutant can not grow on xylose but grows unaffected on glucose as the wild-type
additional information
in-frame deletion mutant can not grow on xylose but grows unaffected on glucose as the wild-type
additional information
-
in-frame deletion mutant can not grow on xylose but grows unaffected on glucose as the wild-type
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
A8BT09
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA subcloned in expression vector pRset, overexpression in Escherichia coli
-
cloned into pET19b, resulting plasmid harvested from Escherichia coli JM109, sequenced, and transformed into Escherichia coli Rosetta(DE3)-pLysS expression strain
gene xyd1, DNA and amino acid sequence determination and analysis, functional expression of the His-tagged enzyme in Saccharomyces cerevisiae
A8BT09
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
production of up to19 g D-xylonate per litre in Kluyveromyces lactis expressing gene xyd1 upon growth on D-galactosel and D-xylose. D-Xylose uptake is not affected by deletion of either the D-xylose reductase XYL1 or a putative xylitol dehydrogenase encoding gene XYL2 in xyd1 expressing strains
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wissler, J.H.
D-Xylose:NADP+ oxidoreductase of arterial vessels and eye lens: a new enzyme and a final link in ATP-independent cycling of reducing equivalents in aldose-polyol-ketose interconvention
Hoppe-Seyler's Z. Physiol. Chem.
358
1300-1301
1977
Bos taurus, Canis lupus familiaris, Sus scrofa
-
brenda
Suzuki, T.; Onishi, H.
Oxidation and reduction of D-xylose by cell-free extract of Pichia quercuum
Appl. Microbiol.
25
850-852
1973
Starmera quercuum
brenda
Zepeda, S.; Monasterio, O.; Ureta, T.
NADP(+)-dependent D-xylose dehydrogenase from pig liver. Purification and properties
Biochem. J.
266
637-644
1990
Sus scrofa
brenda
Asada, Y.; Aoki, S.; Ishikura, S.; Usami, N.; Hara, A.
Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function
Biochem. Biophys. Res. Commun.
278
333-337
2000
Macaca fuscata
brenda
Aoki, S.; Ishikura, S.; Asada, Y.; Usami, N.; Hara, A.
Identity of dimeric dihydrodiol dehydrogenase as NADP+-dependent D-xylose dehydrogenase in pig liver
Chem. Biol. Interact.
130-132
775-784
2001
Canis lupus familiaris, Homo sapiens, Macaca fuscata, Oryctolagus cuniculus, Sus scrofa
brenda
Johnsen, U.; Schonheit, P.
Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui
J. Bacteriol.
186
6198-6207
2004
Haloarcula marismortui (Q5UY95)
brenda
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)
brenda
Berghaell, S.; Hilditch, S.; Penttilae, M.; Richard, P.
Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+):D-xylose dehydrogenase
FEMS Microbiol. Lett.
277
249-253
2007
Trichoderma reesei (A8BT09)
brenda
Johnsen, U.; Dambeck, M.; Zaiss, H.; Fuhrer, T.; Soppa, J.; Sauer, U.; Schoenheit, P.
D-xylose degradation pathway in the halophilic archaeon Haloferax volcanii
J. Biol. Chem.
284
27290-27303
2009
Haloferax volcanii (D4GP29), Haloferax volcanii (D4GP30), Haloferax volcanii DS2 (D4GP30)
brenda
Mihasan, M.; Stefan, M.; Hritcu, L.; Artenie, V.; Brandsch, R.
Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1
Res. Microbiol.
164
22-30
2013
Paenarthrobacter nicotinovorans
brenda
Ahmed, Y.; Ibrahim, I.; Khan, J.; Kumosani, T.
Oxidation and reduction of D-xylose by cell-free extract of Hansenula polymorpha
Aust. J. Basic Appl. Sci.
5
95-100
2011
Ogataea angusta
-
brenda
Nygard, Y.; Toivari, M.H.; Penttilae, M.; Ruohonen, L.; Wiebe, M.G.
Bioconversion of d-xylose to d-xylonate with Kluyveromyces lactis
Metab. Eng.
13
383-391
2011
Trichoderma reesei
brenda
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