EC Number   |
Reaction |
Reference |
|---|
   1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
active site residues are Cys138, Val143, His146, Trp191, and Met200, the catalytic tetrad is formed by Asn107, Ser136, Tyr149, and Lys153, substrate binding site structure, enzyme with dual function showing L-xylulose reductase activity and dicarbonyl reductase activity, EC 1.1.1.5 |
657322 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
active site structure |
654968 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities |
656049 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5 |
654438, 656049 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5, the amino acid residues Ser136, Tyr149, and Lys153 form the catalytic triad |
655222 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
immunological analysis revealed that the dicarbonyl/L-xylulose reductase is not identical with the sperm protein P26h |
656841 |
| 1.1.1.10 | xylitol + NADP+ = L-xylulose + NADPH + H+ |
probably identical with EC 1.1.1.5 diacetyl reductase |
287033 |
