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Literature summary extracted from

  • Toh, S.M.; Mankin, A.S.
    An indigenous posttranscriptional modification in the ribosomal peptidyl transferase center confers resistance to an array of protein synthesis inhibitors (2008), J. Mol. Biol., 380, 593-597.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.24
-
Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.12 additional information lack of pseudouridine at position 2504 of 23S rRNA significantly increases the susceptibility of Escherichia coli to peptidyl transferase inhibitors Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.12 Escherichia coli
-
-
-
5.4.99.24 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.24 23S rRNA uridine955/uridine2504/uridine2580
-
Escherichia coli 23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
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Synonyms

EC Number Synonyms Comment Organism
5.4.99.24 RLuc
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.2.12 physiological function some of the indigenous posttranscriptional modifications of rRNA can be viewed as intrinsic antibiotic resistance mechanisms. The lack of pseudouridine at position 2504 of 23S rRNA significantly increases the susceptibility of Escherichia coli to peptidyl transferase inhibitors Escherichia coli
5.4.99.24 malfunction in the rluC- strain, susceptibility to some antibiotics increases dramatically. The most pronounced effects in comparison with the rluC+ control are observed with clindamycin (16-fold), linezolid (8-fold), and tiamulin (4-fold) Escherichia coli