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23S rRNA (adenine2085-N6)-dimethyltransferase

Class of enzymes

Summary

Class of enzymes

FieldValue
Name23S rRNA (adenine2085-N6)-dimethyltransferase
EC_number2.1.1.184

23S rRNA (adenine2085-N6)-dimethyltransferase (, *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. 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

References

  1. (August 1995). "Substrate requirements for ErmC' methyltransferase activity". Journal of Bacteriology.
  2. (February 1989). "Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase". The Journal of Biological Chemistry.
  3. (August 1987). "Site and substrate specificity of the ermC 23S rRNA methyltransferase". Journal of Bacteriology.
  4. (May 1998). "Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria". Biochemistry.
  5. (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.
  6. (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.
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ec-2.1.1
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