23S rRNA (adenine2085-N6)-dimethyltransferase

23S rRNA (adenine^2085-N^6)-dimethyltransferase
Identifiers
EC number	2.1.1.184
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 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

1. Zhong, P.; Pratt, S.D.; Edalji, R.P.; Walter, K.A.; Holzman, T.F.; Shivakumar, A.G.; Katz, L. (1995). "Substrate requirements for ErmC′ methyltransferase activity". J. Bacteriol. 177: 4327–4332. PMID 7543473.
2. Denoya, C.; 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.
3. Denoya, C.D.; Dubnau, D. (1987). "Site and substrate specificity of the ermC 23S rRNA methyltransferase". J. Bacteriol. 169: 3857–3860. PMID 2440853.
4. 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.; 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.
5. Schluckebier, G.; Zhong, P.; Stewart, K.D.; Kavanaugh, T.J.; 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.
6. Maravic, G.; Bujnicki, J.M.; Feder, M.; Pongor, S.; 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.

External links

• 23S rRNA (adenine2085-N6)-dimethyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)