EC Number   |
General Information |
Reference |
|---|
    1.17.4.1 | malfunction |
wild-type plants exposed to a low concentration of an RNR inhibitor, hydroxyurea, produce chlorotic leaves without growth retardation, reminiscent of v3 and st1 mutants. Upon insufficient activity of RNR, plastid DNA synthesis is preferentially arrested to allow nuclear genome replication in developing leaves, leading to continuous plant growth |
706308 |
| 1.17.4.1 | metabolism |
constitutive ribonucleotide reductase activity ensures stable and balanced dNTP production, which is essential for de novo DNA synthesis. The enzyme is responsible for the rate-limiting step of de novo DNA synthesis |
744958 |
| 1.17.4.1 | metabolism |
constitutive RNR activity ensures stable and balanced dNTP production, which is essential for de novo DNA synthesis. The enzyme is responsible for the rate-limiting step of de novo DNA synthesis |
744958 |
| 1.17.4.1 | metabolism |
key enzyme in DNA synthesis and cell growth control |
744504 |
| 1.17.4.1 | metabolism |
provides the precursors necessary for DNA synthesis. Constitutive ribonucleotide reductase activity ensures stable and balanced dNTP production, which is essential for de novo DNA synthesis. The enzyme is responsible for the rate-limiting step of de novo DNA synthesis |
744958 |
| 1.17.4.1 | metabolism |
the enzyme maintains balanced pools of deoxyribonucleotide substrates for DNA replication by converting ribonucleoside diphosphates to 2'-deoxyribonucleoside diphosphates |
744359 |
| 1.17.4.1 | metabolism |
the reduction of ribonucleoside diphosphate to deoxyribonucleoside diphosphate is the rate-limiting step in dNTP production |
745680 |
| 1.17.4.1 | more |
as the pH is elevated, the rate-determining step of RNR can be altered from a conformational change to proton-coupled electron transfer, and the altered driving force for F3Y oxidation, by residues adjacent to it in the pathway, is responsible for this change |
714233 |
| 1.17.4.1 | more |
comparative analyses of ribonucleotide reductase homologs. Results of homology modeling studies indicate that most of the bifidobacteria-specific conserved signature indels are located within the surface loops of the ribonucleotide reductases, and of these, a large 43 amino acid insert in the class III ribonucleotide reductase homolog forms an extension of the allosteric regulatory site known to be essential for protein function. Preliminary docking studies suggest that this large conserved signature indels may be playing a role in enhancing the stability of the RNR dimer complex |
-, 744978 |
| 1.17.4.1 | more |
RNR and the dNTP-synthesizing complex are closely linked to the replication proteins or replisome at the replication fork, coordinated organization of NrdB protein, and consequently RNR protein, with other replication proteins. NrdB is present in nucleoid-associated clusters during the replication period. These clusters disappear after replication ends. Replication hyperstructure model, overview |
714622 |
