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Literature summary for 1.1.1.307 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

Protein Variants Comment Organism
K274M site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
K74M/N276D site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
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
N276D site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xylitol + NAD+ Saccharomyces cerevisiae
-
D-xylose + NADH + H+
-
r
xylitol + NADP+ Saccharomyces cerevisiae
-
D-xylose + NADPH + H+ NADPH is the preferred cofactor r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
xylose reductase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADP+
-
Saccharomyces cerevisiae
NADPH preferred cofactor Saccharomyces cerevisiae