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Literature summary for 1.1.1.9 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 engineered D202A/L203R/V204S/E205P/S206R mutant enzyme fron Galactocandida mastotermitis with altered cofactor specificity, co-expression with a mutant NADPH-specific xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview Candida sp. HA 167

Protein Variants

Protein Variants Comment Organism
D202A/L203R/V204S/E205P/S206R site-directed mutagenesis, introduction of multiple site-directed mutations in the coenzyme-binding pocket of Galactocandida mastotermitis XDH to enable activity with NADP+, which is lacking in the wild-type enzyme, 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 Candida sp. HA 167

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis of wild-type and mutant enzymes, overview Candida sp. HA 167

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xylitol + NAD+ Candida sp. HA 167
-
D-xylulose + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Candida sp. HA 167
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xylitol + NAD+
-
Candida sp. HA 167 D-xylulose + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
XDH
-
Candida sp. HA 167
xylitol dehydrogenase
-
Candida sp. HA 167

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Candida sp. HA 167

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on, the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction Candida sp. HA 167
NADP+ the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction Candida sp. HA 167