EC Number   |
Inhibitors  |
Structure |
|---|
   2.7.7.8 | 5-Fluorouridine diphosphate |
- |
   |
| 2.7.7.8 | 6-azauridine |
- |
|
| 2.7.7.8 | Acridine orange |
- |
|
| 2.7.7.8 | Acridine orange |
inhibition of polymerization |
|
| 2.7.7.8 | ADP |
inhibits ADP-phosphate exchange |
|
| 2.7.7.8 | ATP |
1.6 mM, 25% inhibition of ADP polymerization |
|
| 2.7.7.8 | ATP |
5 mM, 28°C, presence of MgCl2, 30% residual activity. Allosteric inhibition of both polymerization and phosphorolytic activities, mixed-type inhibition toward phosphate |
|
| 2.7.7.8 | beta,gamma-Imido-ATP |
5 mM, 28°C, presence of MgCl2, 50% residual activity |
|
| 2.7.7.8 | chlortetracycline |
competitive inhibition of ADP polymerization |
|
| 2.7.7.8 | citrate |
a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. PNPase-dependent cells show reduced growth in the presence of increased citrate concentration. In vitro, citrate directly binds and modulates PNPase activity, and the enzyme is inhibited by binding of metal-chelated citrate, predominantly complexed as magnesium-citrate, in the active site at physiological concentrations. In the contrary, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity |
|
