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. 1978 Jul;14(1):105–111. doi: 10.1128/aac.14.1.105

Chloramphenicol Acetyltransferase of Bacteroides fragilis

M L Britz 1, R G Wilkinson 1
PMCID: PMC352412  PMID: 28690

Abstract

Chloramphenicol-resistant strains of Bacteroides 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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