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Literature summary for 2.1.1.224 extracted from

  • Hansen, L.H.; Vester, B.
    A cfr-like gene from Clostridium difficile confers multiple antibiotic resistance by the same mechanism as the cfr gene (2015), Antimicrob. Agents Chemother., 59, 5841-5843.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.224

Cloned(Commentary)

Cloned (Comment) Organism
gene cfr, The Cfr-like protein in Peptoclostridium difficile is hosted by a transposon, and the same gene is found in other strains, sequence comparisons, overview. Recombinant expression in Escherichia coli strain AS19 which then shows elevated MIC values for five classes of antibiotics, and recombinant expression in rlmN-deficient Escherichia coli strain JW2505-1 Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Clostridioides difficile
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 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
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 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile V5ZEZ1 formerly Clostridium difficile, gene cfr
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Clostridioides difficile S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
Cfr
-
 Clostridioides difficile
Cfr-like protein
-
 Clostridioides difficile

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Clostridioides difficile
S-adenosyl-L-methionine
-
 Clostridioides difficile

General Information

General Information Comment Organism
physiological function the Cfr RNA methyltransferase causes multiple resistances to peptidyl transferase inhibitors by methylation of A2503 23S rRNA Clostridioides difficile