EC Number   |
Activating Compound |
Reference |
|---|
    3.6.1.1 | 5',5-P1,P4-diadenosine polyphosphate |
Ap4A, unique as a regulator of CBS-PPase because it bridges two Bateman modules in the dimeric enzyme. It binds non-cooperatively |
755899 |
| 3.6.1.1 | ATP |
- |
755899 |
| 3.6.1.1 | ATP |
1.6fold activation at 0.1 mM |
684988 |
| 3.6.1.1 | ATP |
ATP activates hydrolysis of MgPPi by E-PPase, molecular docking and kinetic analysis involving Lys112 and Lys115, activation mechanism, and regulatory function of ATP, modelling, overview |
685305 |
| 3.6.1.1 | ATP |
CBS-PPases will consume diphosphate more efficiently at high ATP concentrations when biosynthetic reactions proceed faster and produce more diphosphate |
756721 |
| 3.6.1.1 | Diadenosine tetraphosphate |
the structures of the CBSPPase regulatory part contain AMP or diadenosine tetraphosphate (Ap4A) bound to the CBS domains in different modes. AMP is bound in each monomeric unit at the interface between its CBS domains, whereas one Ap4A molecule occupies both AMP-binding sites. The conformational states of the AMP- and Ap4A-bound CBS modules are significantly different, explaining the different effects of the nucleotides on enzyme activity |
756721 |
| 3.6.1.1 | diphosphate |
diphosphate binds Mg2+ to form a true substrate that activates the enzyme |
689923 |
| 3.6.1.1 | dithiothreitol |
- |
657244 |
| 3.6.1.1 | EDTA |
89% activation at 0.9 mM, complete inhibition at 5 mM |
688745 |
| 3.6.1.1 | GSH |
activates up to 4 mM, and inhibits at higher concentrations |
684755 |
