23S rRNA (adenine2503-C2)-methyltransferase

23S rRNA (adenine2503-C2)-methyltransferase
Identifiers
EC number 2.1.1.192
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

23S rRNA (adenine2503-C2)-methyltransferase (EC 2.1.1.192, RlmN, YfgB, Cfr) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA

23S rRNA (adenine2503-C2)-methyltransferase contains an [4Fe-4S] cluster.

References

  1. Toh, S.M.; Xiong, L.; Bae, T.; Mankin, A.S. (2008). "The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA". RNA. 14 (1): 98–106. doi:10.1261/rna.814408. PMC 2151032Freely accessible. PMID 18025251.
  2. Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG (2010). "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA". J. Am. Chem. Soc. 132 (11): 3953–3964. doi:10.1021/ja910850y. PMC 2859901Freely accessible. PMID 20184321.
  3. Yan, F.; Fujimori, D.G. (2011). "RNA methylation by Radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift". Proc. Natl. Acad. Sci. USA. 108 (10): 3930–3934. doi:10.1073/pnas.1017781108. PMC 3054002Freely accessible. PMID 21368151.
  4. Grove, T.L.; Benner, J.S.; Radle, M.I.; Ahlum, J.H.; Landgraf, B.J.; Krebs, C.; Booker, S.J. (2011). "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases". Science. 332 (6029): 604–607. doi:10.1126/science.1200877. PMID 21415317.
  5. Boal, A.K.; Grove, T.L.; McLaughlin, M.I.; Yennawar, N.H.; Booker, S.J.; Rosenzweig, A.C. (2011). "Structural basis for methyl transfer by a radical SAM enzyme". Science. 332 (6033): 544–545. doi:10.1126/science.1205358. PMID 21527678.

External links

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