EC |
2.1.1.226 |
Accepted name: |
23S rRNA (cytidine1920-2′-O)-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA = S-adenosyl-L-homocysteine + 2′-O-methylcytidine1920 in 23S rRNA |
Other name(s): |
TlyA (ambiguous) |
Systematic name: |
S-adenosyl-L-methionine:23S rRNA (cytidine1920-2′-O)-methyltransferase |
Comments: |
The bifunctional enzyme from Mycobacterium tuberculosis 2′-O-methylates cytidine1920 in helix 69 of 23S rRNA and cytidine1409 in helix 44 of 16S rRNA (cf. EC 2.1.1.227, 16S rRNA (cytidine1409-2′-O)-methyltransferase). These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
1. |
Johansen, S.K., Maus, C.E., Plikaytis, B.B. and Douthwaite, S. Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2′-O-methylations in 16S and 23S rRNAs. Mol. Cell 23 (2006) 173–182. [DOI] [PMID: 16857584] |
2. |
Maus, C.E., Plikaytis, B.B. and Shinnick, T.M. Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 49 (2005) 571–577. [DOI] [PMID: 15673735] |
|
[EC 2.1.1.226 created 2011] |
|
|
|
|