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Literature summary extracted from
- Amino acid substitutions in the yeast Pichia stipitis xylitol dehydrogenase coenzyme-binding domain affect the coenzyme specificity (1995), Eur. J. Biochem., 228, 50-54.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.1.10 | additional information | several mutants per site-directed mutagenesis to change the coenzyme binding specificity, mutants showed reduced NAD+ specificity | Scheffersomyces stipitis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.10 | Scheffersomyces stipitis | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.10 | xylitol + NADP+ | - |
Scheffersomyces stipitis | L-xylulose + NADPH + H+ | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.10 | xylitol dehydrogenase | - |
Scheffersomyces stipitis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.10 | NAD+ | preference for, coenzyme-binding domain is a beta-alpha-beta-fold typical for NAD+ dehydrogenases | Scheffersomyces stipitis | |
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Release 2023.1 (January 2023)
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