ENZYME entry: EC 188.8.131.52
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|23S rRNA (adenine(2503)-C(8))-methyltransferase.
|2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin <=> S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin|
- This enzyme is a member of the 'AdoMet radical' (radical SAM) family.
- S-adenosyl-L-methionine acts as both a radical generator and as the
source of the appended methyl group.
- Cfr is an plasmid-acquired methyltransferase that protects cells from
the action of antibiotics.
- The enzyme methylates adenosine at position 2503 of 23S rRNA by a
radical mechanism, transferring a CH(2) group from S-adenosyl-L-
methionine while retaining the hydrogen at the C-8 position of the
- Cfr first transfers an CH(2) group to a conserved cysteine (Cys(338)
in Staphylococcus aureus), the generated radical from a second
S-adenosyl-L-methionine then attacks the methyl group, exctracting a
- The formed radical forms a covalent intermediate with the adenine
group of the tRNA.
- The enzyme will also methylate 2-methyladenine produced by the action
of EC 184.108.40.206.
|PRIAM enzyme-specific profiles||220.127.116.11|
|KEGG Ligand Database for Enzyme Nomenclature||18.104.22.168|
|IUBMB Enzyme Nomenclature||22.214.171.124|
|MEDLINE||Find literature relating to 126.96.36.199|
|Q5WJ42, CFR_BACSK; ||A7Z1T2, CFR_BACVZ; ||A7FX96, CFR_CLOB1; |
|A5I5U3, CFR_CLOBH; ||B1IL14, CFR_CLOBK; ||A7GH77, CFR_CLOBL; |
|B1KZ37, CFR_CLOBM; ||A9KK15, CFR_LACP7; ||A5HBL2, CFR_STAAU; |
|Q9FBG4, CFR_STASC; ||A2AXI2, CFR_STAWA; |
entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
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