Literature summary for 1.1.1.307 extracted from

Bengtsson, O.; Hahn-H�gerdal, B.; Gorwa-Grauslund, M.F.
Xylose reductase from Pichia stipitis with altered coenzyme preference improves ethanolic xylose fermentation by recombinant Saccharomyces cerevisiae (2009), Biotechnol. Biofuels, 2, 904-912.

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Application

Application	Comment	Organism
synthesis	the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation	Scheffersomyces stipitis

Cloned(Commentary)

Cloned (Comment)	Organism
the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation	Scheffersomyces stipitis

Cloned (Comment)

Organism

the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation

Scheffersomyces stipitis

Protein Variants

Protein Variants	Comment	Organism
K270M	mutation results in a significant increase in the Km values for both NADPH and NADH. The kinetic parameters for the NADH-linked reaction catalyzed by the K270M mutant could not even be determined since this mutant could not be saturated with NADH	Scheffersomyces stipitis
K270R	mutation increases the Km value for NADPH 25fold, while the Km for NADH only increased two-fold	Scheffersomyces stipitis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	KM-values determined with crude extracts of native enzyme, mutant enzyme K270M and mutant enzyme K270R	Scheffersomyces stipitis

Organism

Organism	UniProt	Comment	Textmining
Scheffersomyces stipitis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-xylose + NADH + H+	-	Scheffersomyces stipitis	xylitol + NAD+	-	?
D-xylose + NADPH + H+	-	Scheffersomyces stipitis	xylitol + NADP+	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NADH	wild-type enzyme prefers NADPH as cofactor. K270M mutation results in a significant increase in the Km values for both NADPH and NADH. K270R mutation increases the Km value for NADPH 25fold, while the Km for NADH only increases two-fold	Scheffersomyces stipitis
NADPH	wild-type enzyme prefers NADPH as cofactor. K270M mutation results in a significant increase in the Km values for both NADPH and NADH. K270R mutation increases the Km value for NADPH 25fold, while the Km for NADH only increases two-fold	Scheffersomyces stipitis