Information on EC 1.1.1.B64 - xylitol dehydrogenase (NADP+)

for references in articles please use BRENDA:EC1.1.1.B64
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.B64
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
xylitol dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xylitol + NADP+ = D-xylulose + NADPH + H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
xylitol:NADP+ 2-oxidoreductase (D-xylulose-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme mutants D205A/I206R and D205A
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Manually annotated by BRENDA team
enzyme mutants D205A/I206R and D205A
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
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
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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required, the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84. The ligand binding residues for catalytic zinc (residue C46, H71, E72, and E157) and structural zinc (residue C101, C104, C107, and C115) are found in the RpXDH sequence
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.712 - 10.2
NADP+
130
xylitol
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recombinant mutant D205A/I206R, pH 9.0, 35°C, with NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 19.7
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0178 - 0.557
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.026
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crude enzyme extract, pH 8.0, 40°C, substrates xylitol and NADP+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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8% of maximal activity at pH 6.0, maximal activity at pH 8.0, and about 50-60% of maximal activity at pH 8.5-9.0, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 65
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activity range, profile overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87000
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native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from Rhizomucor pusillus strain NBRC 4578 by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration, and a another different step of anion exchange chromatography, ultrafiltration, and gel filtration. The next purification steps are Reactive Red 120 affinity chromatography, dialysis, and ultrafiltration. Recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
D-xylose induces the enzyme expression leading to accumulation of xylitol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D205A
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site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+, cf. EC 1.1.1.9
D205A/I206R
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site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+, cf. EC 1.1.1.9
D205A
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site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+, cf. EC 1.1.1.9
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D205A/I206R
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site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+, cf. EC 1.1.1.9
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production