23S_rRNA_(adenine2503-C2)-methyltransferase

23S rRNA (adenine2503-C2)-methyltransferase

23S rRNA (adenine2503-C2)-methyltransferase

Class of enzymes

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
Quick Facts 2503-C2)-methyltransferase, Identifiers ...

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

References

  1. [1]
    Toh SM, Xiong L, Bae T, Mankin AS (January 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 2151032. PMID 18025251.
  2. [2]
    Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG (March 2010). "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA". Journal of the American Chemical Society. 132 (11): 3953–64. doi:10.1021/ja910850y. PMC 2859901. PMID 20184321.
  3. [3]
    Yan F, Fujimori DG (March 2011). "RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift". Proceedings of the National Academy of Sciences of the United States of America. 108 (10): 3930–4. Bibcode:2011PNAS..108.3930Y. doi:10.1073/pnas.1017781108. PMC 3054002. PMID 21368151.
  4. [4]
    Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ (April 2011). "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases". Science. 332 (6029): 604–7. Bibcode:2011Sci...332..604G. doi:10.1126/science.1200877. PMID 21415317. S2CID 2214309.
  5. [5]
    Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC (May 2011). "Structural basis for methyl transfer by a radical SAM enzyme". Science. 332 (6033): 1089–92. Bibcode:2011Sci...332.1089B. doi:10.1126/science.1205358. PMC 3506250. PMID 21527678.
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