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23S rRNA (adenine2085-N6)-dimethyltransferase
Identifiers
EC no. 2.1.1.184
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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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 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.

External links