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Literature summary extracted from

  • Krahulec, S.; Klimacek, M.; Nidetzky, B.
    Analysis and prediction of the physiological effects of altered coenzyme specificity in xylose reductase and xylitol dehydrogenase during xylose fermentation by Saccharomyces cerevisiae (2012), J. Biotechnol., 158, 192-202.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.9 additional information coenzyme specificities of the NADPH-preferring xylose reductase, EC 1.1.1.307, and the NAD+-dependent xylitol dehydrogenase are targeted in previous studies by protein design or evolution with the aim of improving the recycling of NADH or NADPH in their two-step pathway, converting xylose to xylulose. Yeast strains expressing variant pairs of both enzymes that according to in vitro kinetic data are suggested to be much better matched in coenzyme usage than the corresponding pair of wild-type enzymes, exhibit widely varying capabilities for xylose fermentation, bi-substrate kinetic analysis, and statistical analysis, overview. Engineered strains of Saccharomyces cerevisiae have engineered forms of xylose reductase or xylose dehydrogenase and imporved performance in xylose fermentation Saccharomyces cerevisiae
1.1.1.307 K274M site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.307 K74M/N276D site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
1.1.1.307 additional information coenzyme specificities of the NADPH-preferring xylose reductase and the NAD+-dependent xylitol dehydrogenase, EC 1.1.1.9, are targeted in previous studies by protein design or evolution with the aim of improving the recycling of NADH or NADPH in their two-step pathway, converting xylose to xylulose. Yeast strains expressing variant pairs of both enzymes that according to in vitro kinetic data are suggested to be much better matched in coenzyme usage than the corresponding pair of wild-type enzymes, exhibit widely varying capabilities for xylose fermentation, bi-substrate kinetic analysis, and statistical analysis, overview. Engineered strains of Saccharomyces cerevisiae have engineered forms of xylose reductase or xylose dehydrogenase and improved performance in xylose fermentation Saccharomyces cerevisiae
1.1.1.307 N276D site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.9 additional information
-
 additional information kinetics of mutant enzymes in engineered strains, detailed overview Saccharomyces cerevisiae
1.1.1.307 additional information
-
 additional information kinetics of wild-type and mutant enzymes, detailed overview Saccharomyces cerevisiae
1.1.1.307 0.003
-
 NADPH pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
1.1.1.307 0.017
-
 NADPH pH 7.0, 25°C, mutant N276D Saccharomyces cerevisiae
1.1.1.307 0.026
-
 NADH pH 7.0, 25°C, mutant N276D Saccharomyces cerevisiae
1.1.1.307 0.038
-
 NADH pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
1.1.1.307 0.041
-
 NADH pH 7.0, 25°C, mutant K274M/N276D Saccharomyces cerevisiae
1.1.1.307 0.075
-
 NADPH pH 7.0, 25°C, mutant K274M Saccharomyces cerevisiae
1.1.1.307 0.128
-
 NADPH pH 7.0, 25°C, mutant K274M/N276D Saccharomyces cerevisiae
1.1.1.307 0.38
-
 NADH pH 7.0, 25°C, mutant K274M Saccharomyces cerevisiae
1.1.1.307 96
-
 D-xylose pH 7.0, 25°C, wild-type enzyme, with NADPH Saccharomyces cerevisiae
1.1.1.307 99
-
 D-xylose pH 7.0, 25°C, mutant N276D, with NADH Saccharomyces cerevisiae
1.1.1.307 106
-
 D-xylose pH 7.0, 25°C, mutant K274M/N276D, with NADH Saccharomyces cerevisiae
1.1.1.307 142
-
 D-xylose pH 7.0, 25°C, wild-type enzyme, with NADH Saccharomyces cerevisiae
1.1.1.307 170
-
 D-xylose pH 7.0, 25°C, mutant N276D, with NADPH Saccharomyces cerevisiae
1.1.1.307 229
-
 D-xylose pH 7.0, 25°C, mutant K274M, with NADH Saccharomyces cerevisiae
1.1.1.307 506
-
 D-xylose pH 7.0, 25°C, mutant K274M, with NADPH Saccharomyces cerevisiae
1.1.1.307 722
-
 D-xylose pH 7.0, 25°C, mutant K274M/N276D, with NADPH Saccharomyces cerevisiae

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+ Saccharomyces cerevisiae
-
 D-xylulose + NADH + H+
-
 r
1.1.1.307 xylitol + NAD+ Saccharomyces cerevisiae
-
 D-xylose + NADH + H+
-
 r
1.1.1.307 xylitol + NADP+ Saccharomyces cerevisiae
-
 D-xylose + NADPH + H+ NADPH is the preferred cofactor r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.9 Saccharomyces cerevisiae
-
-
-
1.1.1.307 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.307 xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+ ordered bi-substrate mechanism in which the coenzyme binds first Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.9 xylitol + NAD+
-
 Saccharomyces cerevisiae D-xylulose + NADH + H+
-
 r
1.1.1.307 xylitol + NAD+
-
 Saccharomyces cerevisiae D-xylose + NADH + H+
-
 r
1.1.1.307 xylitol + NADP+
-
 Saccharomyces cerevisiae D-xylose + NADPH + H+ NADPH is the preferred cofactor r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.9 XDH
-
 Saccharomyces cerevisiae
1.1.1.307 xylose reductase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.307 25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.307 3 6 D-xylose pH 7.0, 25°C, mutant K274M, with NADPH Saccharomyces cerevisiae
1.1.1.307 11
-
 D-xylose pH 7.0, 25°C, wild-type enzyme, with NADH Saccharomyces cerevisiae
1.1.1.307 12
-
 D-xylose pH 7.0, 25°C, mutant K274M/N276D, with NADH Saccharomyces cerevisiae
1.1.1.307 13
-
 D-xylose pH 7.0, 25°C, wild-type enzyme, with NADPH Saccharomyces cerevisiae
1.1.1.307 14
-
 D-xylose pH 7.0, 25°C, mutant N276D, with NADH Saccharomyces cerevisiae
1.1.1.307 19
-
 D-xylose pH 7.0, 25°C, mutant K274M, with NADH Saccharomyces cerevisiae
1.1.1.307 30
-
 D-xylose pH 7.0, 25°C, mutant K274M/N276D, with NADPH Saccharomyces cerevisiae
1.1.1.307 37
-
 D-xylose pH 7.0, 25°C, mutant N276D, with NADPH Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.307 7
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.9 NAD+
-
 Saccharomyces cerevisiae
1.1.1.9 NADH
-
 Saccharomyces cerevisiae
1.1.1.307 NAD+
-
 Saccharomyces cerevisiae
1.1.1.307 NADH
-
 Saccharomyces cerevisiae
1.1.1.307 NADP+
-
 Saccharomyces cerevisiae
1.1.1.307 NADPH preferred cofactor Saccharomyces cerevisiae