Protein Variants | Comment | Organism |
---|---|---|
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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of mutant enzymes in engineered strains, detailed overview | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
xylitol + NAD+ | Saccharomyces cerevisiae | - |
D-xylulose + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
xylitol + NAD+ | - |
Saccharomyces cerevisiae | D-xylulose + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
XDH | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Saccharomyces cerevisiae | |
NADH | - |
Saccharomyces cerevisiae |