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 (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 | 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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Scheffersomyces stipitis | - |
- |
- |
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 | 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 |