| EC |
2.1.1.227 |
| Accepted name: |
16S rRNA (cytidine1409-2′-O)-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + cytidine1409 in 16S rRNA = S-adenosyl-L-homocysteine + 2′-O-methylcytidine1409 in 16S rRNA
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| Other name(s): |
TlyA (ambiguous) |
| Systematic name: |
S-adenosyl-L-methionine:16S rRNA (cytidine1409-2′-O)-methyltransferase |
| Comments: |
The bifunctional enzyme from Mycobacterium tuberculosis 2′-O-methylates cytidine1409 in helix 44 of 16S rRNA and cytidine1920 in helix 69 of 23S rRNA (cf. EC 2.1.1.226, 23S rRNA (cytidine1920-2′-O)-methyltransferase). |
| Links to other databases: |
BRENDA, EXPASY, 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] |
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| [EC 2.1.1.227 created 2011] |
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