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Information on EC 1.1.1.307 - D-xylose reductase [NAD(P)H] and Organism(s) Debaryomyces nepalensis and UniProt Accession A0A0M4HL56

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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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Debaryomyces nepalensis
UNIPROT: A0A0M4HL56
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Word Map
The taxonomic range for the selected organisms is: Debaryomyces nepalensis
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, nad(p)h-linked xylose reductase, nadp-dependent xylose reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)].
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 + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
-
r
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 + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50.2
recombinant enzyme, pH 7.1, 27°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0M4HL56_9ASCO
320
0
36574
TrEMBL
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
simultaneous optimization of xylose reductase activity and stability using statistical methods is effective as compared to optimisation of the parameters separately, effects of pH and temperature on the activity and stability of xylose reductase from Debaryomyces nepalensis NCYC 3413 are investigated by enzyme assays, and independent variables are optimised using surface response methodology. Enzyme activity and stability are optimised separately and concurrently to decipher the appropriate conditions, method comparisons, overview. Optimized conditions are pH 7.1 and 27°C with predicted responses of specific activity of 72.3 U/mg and half-life time of 566 min. The experimental values (specific activity 50.2 U/mg, half-life time 818 min) are on par with predicted values indicating the significance of the model
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malla, S.; Gummadi, S.N.
Simultaneous optimization of activity and stability of xylose reductase from D. nepalensis NCYC 3413 using statistical experimental design
Protein Pept. Lett.
28
489-500
2020
Debaryomyces nepalensis (A0A0M4HL56), Debaryomyces nepalensis NCYC 3413 (A0A0M4HL56)
Manually annotated by BRENDA team