Cloned (Comment) | Organism |
---|---|
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 |
Protein Variants | Comment | Organism |
---|---|---|
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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetic analysis of wild-type and mutant enzymes, overview | Candida sp. HA 167 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
xylitol + NAD+ | Candida sp. HA 167 | - |
D-xylulose + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida sp. HA 167 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
xylitol + NAD+ | - |
Candida sp. HA 167 | D-xylulose + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
XDH | - |
Candida sp. HA 167 |
xylitol dehydrogenase | - |
Candida sp. HA 167 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Candida sp. HA 167 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 |