23S rRNA (cytidine-2'-O)-methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.226 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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23S rRNA (cytidine-2'-O)-methyltransferase (EC 2.1.1.226, TlyA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytidine-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + cytidine in 23S rRNA S-adenosyl-L-homocysteine + 2'-O-methylcytidine in 23S rRNA
This is a bifunctional enzyme from Mycobacterium tuberculosis.
References
- Johansen SK, Maus CE, Plikaytis BB, Douthwaite S (July 2006). "Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs". Molecular Cell. 23 (2): 173–82. doi:10.1016/j.molcel.2006.05.044. PMID 16857584.
- Maus CE, Plikaytis BB, Shinnick TM (February 2005). "Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis". Antimicrobial Agents and Chemotherapy. 49 (2): 571–7. doi:10.1128/AAC.49.2.571-577.2005. PMC 547314. PMID 15673735.
External links
- 23S+rRNA+(cytidine1920-2'-O)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Transferase: one carbon transferases (EC 2.1) | |||||||||
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2.1.1: Methyl- |
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2.1.2: Hydroxymethyl-, Formyl- and Related |
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2.1.3: Carboxy- and Carbamoyl |
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2.1.4: Amidine |
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