EC 2.1.1.226 - 23S rRNA (cytidine1920-2'-O)-methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.226

Names

Accepted name:
23S rRNA (cytidine1920-2'-O)-methyltransferase
Other name:
TlyA [ambiguous]
Systematic name:
S-adenosyl-L-methionine:23S rRNA (cytidine1920-2'-O)-methyltransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Johansen, S. K., Maus, C. E., Plikaytis, B. B., Douthwaite, S.
    Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs.
    Mol. Cell 23: 173-182 (2006). [PMID: 16857584]
  2. Maus, C. E., Plikaytis, B. B., Shinnick, T. M.
    Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis.
    Antimicrob. Agents Chemother. 49: 571-577 (2005). [PMID: 15673735]

[EC 2.1.1.226 created 2011]