Any feedback?
Literature summary for 1.1.1.431 extracted from
- Mutational study of the role of tyrosine-49 in the Saccharomyces cerevisiae xylose reductase (2001), Yeast, 18, 1081-1089.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y49F | more than 98% loss of activity compared to wild-type enzyme | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.6 | - |
NADPH | pH 7.0, 22°C, wild-type enzyme | Saccharomyces cerevisiae |  |
| 14.8 | - |
D-xylose | pH 7.0, 22°C, wild-type enzyme | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 37000 | - |
x * 37000, wild-type and mutant enzyme Y49F, SDS-PAGE | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type and mutant enzyme Y49F | Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2 | - |
mutant enzyme Y49F | Saccharomyces cerevisiae |
| 104 | - |
wild-type enzyme | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-xylose + NADH + H+ | - |
Saccharomyces cerevisiae | xylitol + NAD+ | - |
? | |
| D-xylose + NADPH + H+ | - |
Saccharomyces cerevisiae | xylitol + NADP+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 37000, wild-type and mutant enzyme Y49F, SDS-PAGE | Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13.1 | - |
D-xylose | pH 7.0, 22°C, wild-type enzyme | Saccharomyces cerevisiae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | prefers NADPH as the coenzyme by about 80fold over NADH | Saccharomyces cerevisiae | |
| NADPH | prefers NADPH as the coenzyme by about 80fold over NADH | Saccharomyces cerevisiae | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.89 | - |
D-xylose | pH 7.0, 22°C, wild-type enzyme | Saccharomyces cerevisiae | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
