EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.2.8 | QM/MM simulations. The relatively stronger hydrogen-bond interactions between uridine and the active-site residues Gln227 and Tyr231 play an important role in enhancing the substrate binding and thus promoting the N-glycosidic bond cleavage, in comparison with inosine. The estimated energy barrier is 30 kcal/mol for the hydrolysis of inosine and 22 kcal/mol for uridine. The uridine binding is exothermic by about 23 kcal/mol, and inosine binding by 12 kcal/mol | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.2.8 | Escherichia coli | C3T3U2 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.2.8 | YeiK | - |
Escherichia coli |