EC Number   |
Activating Compound |
Reference |
|---|
    1.17.4.1 | 2-mercaptoethanol |
25 mM, maximal activation, 70% of activity with dithiothreitol |
437977 |
| 1.17.4.1 | adenyl-5'-yl-imidodiphosphate |
can replace ATP as activator of CDP and UDP reduction |
437933 |
| 1.17.4.1 | adenyl-5'-yl-imidodiphosphate |
maximal activation of CDP reduction at 4 mM |
437907 |
| 1.17.4.1 | adenyl-5'-yl-imidodiphosphate |
stimulation at low concentration, inhibition above 0.3 mM |
437974 |
| 1.17.4.1 | ADP |
- |
437933 |
| 1.17.4.1 | ATP |
- |
437918, 437937, 437969, 437988, 685235, 686735, 688589, 702161, 702551, 704612, 714233 |
| 1.17.4.1 | ATP |
activates |
714258 |
| 1.17.4.1 | ATP |
activation by ATP has a regulatory function |
716317 |
| 1.17.4.1 | ATP |
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes |
745325 |
| 1.17.4.1 | ATP |
allosteric effector of CDP reaction |
744504 |
