EC Number   |
General Information |
Reference |
|---|
    1.1.98.6 | physiological function |
during the reduction of ribonucleotides with [3H]formate tritium appears in water and not in the product deoxyribonucleotide. In D2O, deuterium replaces the OH-group at carbon-2' with retention of configuration. Class I, II and class III enzymes catalyze identical reactions. Members of the three classes of reductases apparently use the same chemical mechanism in spite of having completely different protein structures |
739975 |
| 1.1.98.6 | physiological function |
protein NrdD contains catalytic and allosteric sites and, in its active form, a stable glycyl radical. This radical is generated by NrdG with its [4Fe-4S] cluster and S-adenosylmethionine. NrdD and NrdG anaerobically form a tight alpha2beta2 complex. NrdD alone catalyzes the reduction of CTP with formate as the electron donor and ATP as the allosteric effector. The reaction requires Mg+ and is stimulated by K+ but not by dithiothreitol. NrdD is the actual reductase, and NrdG is an activase |
740670 |
| 1.1.98.6 | physiological function |
proteins NrdG and NrdD together catalyze the reduction of ribonucleoside triphosphates to the corresponding deoxyribonucleotides in the presence of S-adenosylmethionine, reduced flavodoxin or reduced deazaflavin, potassium ions, dithiothreitol, and formate. A [4Fe-4S] cluster is present in reduced NrdG and a glycyl radical in activated NrdD. The two polypeptides of NrdD and the proteins in the NrdD-NrdG complex are only loosely associated. NrdDG is required for strict anaerobic growth of Lactococcus lactis |
740670 |
| 1.1.98.6 | physiological function |
the enzyme is the actual ribonucleoside triphosphate reductase in the oxygen-sensitive ribonucleoside triphosphate reductase system. The reaction requires an auxiliary protein dA1 of 29000 Da, S-adenosylmethionine, NADPH (with NADH as a less active substitute), dithinthreitol, and magnesium ions, and is strongly stimulated by ATP |
740651 |
