23S rRNA (adenine2085-N6)-dimethyltransferase
23S rRNA (adenine2085-N6)-dimethyltransferase (EC 2.1.1.184, ErmC' methyltransferase, ermC methylase, ermC 23S rRNA methyltransferase, rRNA:m6A methyltransferase ErmC', ErmC', rRNA methyltransferase ErmC' ) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2085-N6)-dimethyltransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- 2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA
2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalysing the methylation of 23S rRNA at adenine2085.
References
- ↑ Zhong, P., Pratt, S.D., Edalji, R.P., Walter, K.A., Holzman, T.F., Shivakumar, A.G. and Katz, L. (1995). "Substrate requirements for ErmC′ methyltransferase activity". J. Bacteriol. 177: 4327–4332. PMID 7543473.
- ↑ Denoya, C. and Dubnau, D. (1989). "Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase". J. Biol. Chem. 264: 2615–2624. PMID 2492520.
- ↑ Denoya, C.D. and Dubnau, D. (1987). "Site and substrate specificity of the ermC 23S rRNA methyltransferase". J. Bacteriol. 169: 3857–3860. PMID 2440853.
- ↑ Bussiere, D.E., Muchmore, S.W., Dealwis, C.G., Schluckebier, G., Nienaber, V.L., Edalji, R.P., Walter, K.A., Ladror, U.S., Holzman, T.F. and Abad-Zapatero, C. (1998). "Crystal structure of ErmC′, an rRNA methyltransferase which mediates antibiotic resistance in bacteria". Biochemistry 37: 7103–7112. doi:10.1021/bi973113c. PMID 9585521.
- ↑ Schluckebier, G., Zhong, P., Stewart, K.D., Kavanaugh, T.J. and Abad-Zapatero, C. (1999). "The 2.2 Å structure of the rRNA methyltransferase ErmC′ and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism". J. Mol. Biol. 289: 277–291. doi:10.1006/jmbi.1999.2788. PMID 10366505.
- ↑ Maravic, G., Bujnicki, J.M., Feder, M., Pongor, S. and Flogel, M. (2003). "Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC′ redefines the substrate-binding site and suggests a model for protein-RNA interactions". Nucleic Acids Res. 31: 4941–4949. doi:10.1093/nar/gkg666. PMID 12907737.
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