Biology:23S rRNA (adenine2085-N6)-dimethyltransferase
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Short description: Class of enzymes
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Substrate requirements for ErmC' methyltransferase activity". Journal of Bacteriology 177 (15): 4327–32. August 1995. PMID 7543473.
- ↑ "Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase". The Journal of Biological Chemistry 264 (5): 2615–24. February 1989. PMID 2492520.
- ↑ "Site and substrate specificity of the ermC 23S rRNA methyltransferase". Journal of Bacteriology 169 (8): 3857–60. August 1987. PMID 2440853.
- ↑ "Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria". Biochemistry 37 (20): 7103–12. May 1998. doi:10.1021/bi973113c. PMID 9585521.
- ↑ "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. June 1999. doi:10.1006/jmbi.1999.2788. PMID 10366505.
- ↑ "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. August 2003. 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)
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