EC Number   |
Activating Compound |
Reference |
|---|
    2.4.2.9 | alendronate |
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.5fold, increases the initial rate of synthesis of UMP 2.3fold |
685041 |
| 2.4.2.9 | ATP |
weak activation |
678368 |
| 2.4.2.9 | clodronate |
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2fold, increases the initial rate of synthesis of UMP 1.9fold |
685041 |
| 2.4.2.9 | dGTP |
highly activating, no effect on Km values |
638368 |
| 2.4.2.9 | etidronate |
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.8fold, increases the initial rate of synthesis of UMP 2.1fold |
685041 |
| 2.4.2.9 | glutathione |
omission of glutathione reduces the reaction rate about 25% |
638358 |
| 2.4.2.9 | GTP |
about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax |
638369, 638374 |
| 2.4.2.9 | GTP |
activating allosteric regulation by GTP. The regulatory triphosphate binds at a site in the center of the tetramer changing the quaternary arrangement. The effector contacts Pro94 at the beginning of a long beta-strand in the dimer interface, which extends into a flexible loop over the active site. In the GTP-bound state, two flexible loop residues, Tyr123 and Lys125, bind the diphosphate moiety of PRPP in the neighboring subunit and contribute to catalysis. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state |
705159 |
| 2.4.2.9 | GTP |
activation of wild-type and mutant P131D, maximal at 0.08 mM |
638372 |
| 2.4.2.9 | GTP |
activation, stabilization of the tetrameric structure at 2 mM, without GTP enzyme forms dimers |
638374 |
