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Literature summary extracted from
- Examination of the mechanism and energetic contribution of leaving group activation in the purine-specific nucleoside hydrolase from Trypanosoma vivax (2007), Biochim. Biophys. Acta, 1774, 1451-1461.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.2.1 | Trypanosoma vivax | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.2.2.1 | a purine nucleoside + H2O = D-ribose + a purine base | ordered bi-bi kinetic mechanism and high forward commitment with inosine as substrate. The dominant energetic contribution towards catalysis comes from ribosyl and water activation, leaving group activation also makes a considerable contribution. The leaving group is unlikely to be protonated prior to N-glycosidic bond cleavage and active site binding interactions to the purine leaving group are required for efficient ribosyl and/or water activation | Trypanosoma vivax |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.1 | 4-nitrophenylriboside + H2O | - |
Trypanosoma vivax | 4-nitrophenol + D-ribose | - |
? |  |
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