23S rRNA (adenine2085-N6)-dimethyltransferase

23S rRNA (adenine2085-N6)-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

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

  1. ↑ Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L (August 1995). "Substrate requirements for ErmC' methyltransferase activity". Journal of Bacteriology. 177 (15): 4327–32. PMC 177180. PMID 7543473.
  2. ↑ Denoya C, Dubnau D (February 1989). "Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase". The Journal of Biological Chemistry. 264 (5): 2615–24. PMID 2492520.
  3. ↑ Denoya CD, Dubnau D (August 1987). "Site and substrate specificity of the ermC 23S rRNA methyltransferase". Journal of Bacteriology. 169 (8): 3857–60. PMC 212483. PMID 2440853.
  4. ↑ Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C (May 1998). "Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria". Biochemistry. 37 (20): 7103–12. doi:10.1021/bi973113c. PMID 9585521.
  5. ↑ Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C (June 1999). "The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism". Journal of Molecular Biology. 289 (2): 277–91. doi:10.1006/jmbi.1999.2788. PMID 10366505.
  6. ↑ Maravić G, Bujnicki JM, Feder M, Pongor S, Flögel M (August 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 Research. 31 (16): 4941–9. doi:10.1093/nar/gkg666. PMC 169915. PMID 12907737.
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