| ribonucleoside-diphosphate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Ribonucleoside-diphosphate reductase heterooctamer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 1.17.4.1 | ||||||||
| CAS no. | 9047-64-7sy | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides.[1][2] It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates (or triphosphates depending on the class of RNR). This reduction produces deoxyribonucleotides.[3] Deoxyribonucleotides in turn are used in the synthesis of DNA. The reaction catalyzed by RNR is strictly conserved in all living organisms.[4] 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.[5] A somewhat unusual feature of the RNR enzyme is that it catalyzes a reaction that proceeds via a free radical mechanism of action.[6][7] The substrates for RNR are ADP, GDP, CDP and UDP. dTDP (deoxythymidine diphosphate) is synthesized by another enzyme (thymidylate kinase) from dTMP (deoxythymidine monophosphate).
- ^ Hofer A, Crona M, Logan DT, Sjöberg BM (2012). "DNA building blocks: keeping control of manufacture". Critical Reviews in Biochemistry and Molecular Biology. 47 (1): 50–63. doi:10.3109/10409238.2011.630372. PMC 3267527. PMID 22050358.
- ^ Elledge SJ, Zhou Z, Allen JB (March 1992). "Ribonucleotide reductase: regulation, regulation, regulation". Trends in Biochemical Sciences. 17 (3): 119–23. doi:10.1016/0968-0004(92)90249-9. PMID 1412696.
- ^ 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.