EC Number   |
Reaction |
Reference |
|---|
    2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
active site structure |
638406, 638407, 638412, 638417, 638419, 638422, 638423 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
binding structure involving residue K68 at the AB-dimer interface and residues V96 and D97 of the opposing subunit, overview. Residues E133 and D137 block the binding of 5-phospho-alpha-D-ribose 1-diphosphate, mechanism, overview |
705998 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
catalytic mechanism |
638406, 638407, 638409, 638412, 638417, 638418, 638422 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
during catalysis a long flexible loop closes over the active site, functional role |
638419 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
essential role of Ser95-Tyr96 dyade in catalysis |
638408 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
guanine and 6-mercaptopurine can replace hypoxanthine |
- |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
kinetic mechanism |
638409 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
kinetic model |
638410 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
ordered bi bi kinetic mechanism with 5-phospho-alpha-D-ribose 1-diphosphate binding first followed by the purine base |
661691 |
| 2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate |
ordered bi bi reaction mechanism, formation of dead-end complexes with purine substrates and diphosphate |
661245 |
