Biology:23S rRNA (adenine2503-C2)-methyltransferase

From HandWiki
Short description: Class of enzymes
23S rRNA (adenine2503-C2)-methyltransferase
Identifiers
EC number2.1.1.192
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA". RNA 14 (1): 98–106. January 2008. doi:10.1261/rna.814408. PMID 18025251. 
  2. "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA". Journal of the American Chemical Society 132 (11): 3953–64. March 2010. doi:10.1021/ja910850y. PMID 20184321. 
  3. "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. March 2011. doi:10.1073/pnas.1017781108. PMID 21368151. Bibcode2011PNAS..108.3930Y. 
  4. "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases". Science 332 (6029): 604–7. April 2011. doi:10.1126/science.1200877. PMID 21415317. Bibcode2011Sci...332..604G. 
  5. "Structural basis for methyl transfer by a radical SAM enzyme". Science 332 (6033): 1089–92. May 2011. doi:10.1126/science.1205358. PMID 21527678. Bibcode2011Sci...332.1089B. 

External links