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Literature summary for 1.1.1.431 extracted from

  • Krahulec, S.; Klimacek, M.; Nidetzky, B.
    Engineering of a matched pair of xylose reductase and xylitol dehydrogenase for xylose fermentation by Saccharomyces cerevisiae (2009), Biotechnol. J., 4, 684-694.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of the mutant xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, co-expression with an engineered xylitol dehydrogenase, with altered cofactor specificity, from Galactocandida mastotermitis, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview Yamadazyma tenuis

Protein Variants

Protein Variants Comment Organism
additional information the mutant Candida tenuis enzyme is modified in its cofactor specificity showing preference for NADPH compared to NADH in the D-xylose reduction reaction, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview Yamadazyma tenuis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-xylose + NAD(P)H + H+ Yamadazyma tenuis
-
xylitol + NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.16 0.4 recombinant enzyme in transgenic strains of Saccharomyces cerevisiae Yamadazyma tenuis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NAD(P)H + H+
-
Yamadazyma tenuis xylitol + NAD(P)+
-
?

Synonyms

Synonyms Comment Organism
NAD(P)H-dependent xylose reductase
-
Yamadazyma tenuis
xylose reductase
-
Yamadazyma tenuis

Cofactor

Cofactor Comment Organism Structure
NAD(P)H dependent on, the wild-type enzyme prefers NADH, while a modified mutant enzyme prefers NADPH in the D-xylose reduction reaction Yamadazyma tenuis