EC Number   |
Natural Substrates |
|---|
   2.1.1.224 | 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA |
- |
| 2.1.1.224 | 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA |
Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics |
| 2.1.1.224 | 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA |
the enzyme methylates the 8 position of 23S rRNA residue A2503 to confer resistance to multiple antibiotic classes acting upon the large subunit of the bacterial ribosome |
| 2.1.1.224 | 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin |
- |
| 2.1.1.224 | 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin |
- |
| 2.1.1.224 | more |
Cfr confers a phenotype with resistance to phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A antibiotics. Methylation of position 8 is the dominant antibiotic resistance determinant, but indigenous modification at position 2 also contributes to low-level resistance |
| 2.1.1.224 | more |
enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. In wild-type Cfr, where Cys338 is methylated, S-adenosyl-L-methionine binding leads to rapid oxidation of the [4Fe-4S] cluster and production of 5'-deoxyadenosine |
| 2.1.1.224 | more |
methylation at C8 is similar to that at C2, cf. EC 2.1.1.192 |
| 2.1.1.224 | S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin |
- |
