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Information on EC 1.1.1.307 - D-xylose reductase [NAD(P)H] and Organism(s) Candida parapsilosis and UniProt Accession Q6Y0Z3

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EC Tree
IUBMB Comments
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH [cf. EC 1.1.1.431, D-xylose reductase (NADPH)]. However, a few D-xylose reductases, such as those from Neurospora crassa , Yamadazyma tenuis [2,3], Scheffersomyces stipitis , and the thermophilic fungus Chaetomium thermophilum [4,7], have dual coenzyme specificity, though they still prefer NADPH to NADH. Very rarely the enzyme prefers NADH [cf. EC 1.1.1.430, D-xylose reductase (NADH)].
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Candida parapsilosis
UNIPROT: Q6Y0Z3
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Word Map
The taxonomic range for the selected organisms is: Candida parapsilosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
akr2b5, kmxyl1, nad(p)h-dependent xr, nad(p)h-dependent d-xylose reductase, nadp-dependent xylose reductase, nad(p)h-linked xylose reductase, more
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD(P)+ oxidoreductase
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH [cf. EC 1.1.1.431, D-xylose reductase (NADPH)]. However, a few D-xylose reductases, such as those from Neurospora crassa [5], Yamadazyma tenuis [2,3], Scheffersomyces stipitis [1], and the thermophilic fungus Chaetomium thermophilum [4,7], have dual coenzyme specificity, though they still prefer NADPH to NADH. Very rarely the enzyme prefers NADH [cf. EC 1.1.1.430, D-xylose reductase (NADH)].
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XYL1_CANPA
324
0
36629
Swiss-Prot
other Location (Reliability: 2)