Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase (rNDP), is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides.[1] It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates. This reduction produces deoxyribonucleotides.[2] Deoxyribonucleotides in turn are used in the synthesis of DNA. The reaction catalyzed by RNR is strictly conserved in all living organisms.[3] Furthermore, RNR plays a critical role in regulating the total rate of DNA synthesis so that DNA to cell mass is maintained at a constant ratio during cell division and DNA repair.[4] A somewhat unusual feature of the RNR enzyme is that it catalyzes a reaction that proceeds via a free radical mechanism of action.[5][6] The substrates for RNR are ADP, GDP, CDP and UDP. dTDP (deoxythymidine diphosphate) is synthesized by another enzyme (thymidylate kinase) from dTMP (deoxythymidine monophosphate).
^Sneeden JL, Loeb LA (September 2004). "Mutations in the R2 subunit of ribonucleotide reductase that confer resistance to hydroxyurea". The Journal of Biological Chemistry. 279 (39): 40723–8. doi:10.1074/jbc.M402699200. PMID 15262976.
^Torrents E, Aloy P, Gibert I, Rodríguez-Trelles F (August 2002). "Ribonucleotide reductases: divergent evolution of an ancient enzyme". Journal of Molecular Evolution. 55 (2): 138–52. Bibcode:2002JMolE..55..138T. doi:10.1007/s00239-002-2311-7. PMID 12107591. S2CID 24603578.
^Herrick J, Sclavi B (January 2007). "Ribonucleotide reductase and the regulation of DNA replication: an old story and an ancient heritage". Molecular Microbiology. 63 (1): 22–34. doi:10.1111/j.1365-2958.2006.05493.x. PMID 17229208. S2CID 9473163.
^Eklund H, Eriksson M, Uhlin U, Nordlund P, Logan D (August 1997). "Ribonucleotide reductase—structural studies of a radical enzyme". Biological Chemistry. 378 (8): 821–5. doi:10.1515/bchm.1997.378.8.815. PMID 9377477.
^Stubbe J, Riggs-Gelasco P (November 1998). "Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase". Trends in Biochemical Sciences. 23 (11): 438–43. doi:10.1016/S0968-0004(98)01296-1. PMID 9852763.
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