Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. The structural basis for the allosteric regulation of ribonucleotide reductase. Moreover, this enzyme can be considered an ideal target for anti-proliferative compounds designed to inhibit cell replication in eukaryotic cells (cancer cells), parasites, viruses, and bacteria.ĭNA synthesis NrdR anaerobiosis evolution gene regulation ribonucleotide reductase transcriptional regulation.Īhmad M. In this review we examine the distribution, the evolution, and the genetic regulation of bacterial RNRs. Thus, RNR activity should be finely regulated allosterically and at the transcriptional level. The strict control of RNR activity and dNTP pool sizes is important, as pool imbalances increase mutation rates, replication anomalies, and genome instability. Clearly, RNR enzymes have contributed to the appearance of genetic material that exists today, being essential for the evolution of all organisms on Earth. This enzyme converts ribonucleotides to deoxyribonucleotides, the building blocks for DNA replication, and repair. Ribonucleotide reductase (RNR) is a key enzyme that mediates the synthesis of deoxyribonucleotides, the DNA precursors, for DNA synthesis in every living cell.
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