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Literature summary for 2.1.1.224 extracted from

  • Stojkovic, V.; Ulate, M.F.; Hidalgo-Villeda, F.; Aguilar, E.; Monge-Cascante, C.; Pizarro-Guajardo, M.; Tsai, K.; Tzoc, E.; Camorlinga, M.; Paredes-Sabja, D.; Quesada-Gomez, C.; Fujimori, D.G.; Rodriguez, C.
    cfr(B), cfr(C), and a new cfr-like gene, cfr(E), in Clostridium difficile strains recovered across Latin America (2019), Antimicrob. Agents Chemother., 64, e01074-19 .
    View publication on PubMed
Search for more literature for 2.1.1.224

Cloned(Commentary)

Cloned (Comment) Organism
gene cfr(E), DNA and amino acid sequence determination and analysis, genotyping, sequence comparisons and phylogenetic analysis of different cfr gene variants, recombinant expression of tagged enzyme Cfr(E) in Escherichia coli strain Rosetta(DE3)pLysS Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required 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 [2Fe-2S] ferredoxin Clostridioides difficile
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin Clostridioides difficile DF11
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
 clinical isolate from Mexico
-
Clostridioides difficile DF11
-
 clinical isolate from Mexico
-

Purification (Commentary)

Purification (Comment) Organism
recombinant tagged enzyme Cfr(E) from Escherichia coli strain Rosetta(DE3)pLysS by metal chelating chromatography Clostridioides difficile

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Clostridioides difficile S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Clostridioides difficile DF11 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
additional information in vitro assays with Escherichia coli RNA Clostridioides difficile ?
-
-
additional information in vitro assays with Escherichia coli RNA Clostridioides difficile DF11 ?
-
-

Synonyms

Synonyms Comment Organism
Cfr
-
 Clostridioides difficile
Cfr(E)
-
 Clostridioides difficile

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Clostridioides difficile

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Clostridioides difficile

Cofactor

Cofactor Comment Organism Structure
reduced [2Fe-2S] ferredoxin
-
 Clostridioides difficile
S-adenosyl-L-methionine
-
 Clostridioides difficile

General Information

General Information Comment Organism
evolution three cfr-like genes implicated in antibiotic resistance have been described, two of which, cfr(B) and cfr(C), have been sporadically detected in Clostridium difficile. The methylase activity of Cfr(C) has not been confirmed. cfr(B), cfr(C), and a cfr-like genes show only 51 to 58% protein sequence identity to Cfr and Cfr-like enzymes in clinical Clostridium difficile isolates recovered across nearly a decade in Mexico, Honduras, Costa Rica, and Chile. This resistance gene is termed cfr(E). The predicted protein sequence of Cfr(E) shows homology to C8 RNA-methylating enzymes. Enzymes Cfr(C) or Cfr(E) are determined to methylate A2503 at the C8 position. The cfr-like gene of isolate DF11 (Cfr(E))is found integrated into an undescribed MGE that shows partial hits to genomic sequences of various intestinal Firmicutes, but in all cases, shared regions do not include cfr(E) or its adjacent genes, overview Clostridioides difficile
physiological function Cfr is a radical S-adenosyl-L-methionine (SAM) enzyme that confers cross-resistance to antibiotics targeting the 23S rRNA through hypermethylation of nucleotide A2503 Clostridioides difficile