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Chloramphenicol acetyltransferase of bacteroides-fragilis
journal contribution
posted on 2023-05-17, 08:19 authored by Margaret BritzMargaret Britz, Wilkinson, RGChloramphenicol-resistant strains of B. fragilis (minimum inhibitory concentration, 12.5 μg/ml) were isolated from a stool specimen which contained multiply resistant Escherichia coli. The enzyme responsible for resistance, chloramphenicol acetyltransferase, was produced constitutively by these strains; the specific activity was 10-fold lower than that of the E. coli enzymes. Similar activity was not detected in susceptible B. fragilis strains, nor could it be induced by growth in the presence of chloramphenicol or by mutagenesis. The enzyme had a pH optimum of 7.8 and a molecular weight of approximately 89,000. The Km for chloramphenicol was 5.2 μM, and the enzyme was sensitive to inhibition by 5.5'-dithiobis-2-nitrobenzoic acid. The enzyme produced by an E. coli strain isolated from the same specimen had a similar Km and sensitivity to 5.5'-dithiobis-2-nitrobenzoic acid.
History
Publication title
Antimicrobial Agents and ChemotherapyVolume
14Pagination
105-111ISSN
0066-4804Department/School
College Office - College of Sciences and EngineeringPublisher
Amer Soc MicrobiologyPlace of publication
1752 N St Nw, Washington, USA, Dc, 20036-2904Repository Status
- Restricted