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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.9 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
1.1.1.10 expressed in Saccharomyces cerevisiae Yamadazyma tenuis
1.1.1.431 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

EC Number Protein Variants Comment Organism
1.1.1.9 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
1.1.1.431 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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.9 xylitol + NAD+ Candida sp. HA 167
-
 D-xylulose + NADH + H+
-
 ?
1.1.1.431 D-xylose + NAD(P)H + H+ Yamadazyma tenuis
-
 xylitol + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.9 Candida sp. HA 167
-
-
-
1.1.1.10 Yamadazyma tenuis
-
-
-
1.1.1.431 Yamadazyma tenuis
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.431 0.16 0.4 recombinant enzyme in transgenic strains of Saccharomyces cerevisiae Yamadazyma tenuis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.9 xylitol + NAD+
-
 Candida sp. HA 167 D-xylulose + NADH + H+
-
 ?
1.1.1.10 L-xylulose + NADPH + H+
-
 Yamadazyma tenuis L-xylitol + NADP+
-
 ?
1.1.1.431 D-xylose + NAD(P)H + H+
-
 Yamadazyma tenuis xylitol + NAD(P)+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.9 XDH
-
 Candida sp. HA 167
1.1.1.9 xylitol dehydrogenase
-
 Candida sp. HA 167
1.1.1.10 NAD(P)H-dependent xylose reductase
-
 Yamadazyma tenuis
1.1.1.431 NAD(P)H-dependent xylose reductase
-
 Yamadazyma tenuis
1.1.1.431 xylose reductase
-
 Yamadazyma tenuis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.9 7
-
 assay at Candida sp. HA 167

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.9 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
1.1.1.9 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
1.1.1.10 NADPH
-
 Yamadazyma tenuis
1.1.1.431 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