O-Acetyltransferases for chloramphenicol and other natural products

The range of enzymatic mechanisms by which bacteria inactivate biologically active molecules is limited by two kinds of constraint, namely, the structure-activity correlations for each class of chemical agent and the metabolic repertoire available to bacteria. In the case of chloramphenicol (Cml), which, given its size, has a wealth of vulnerable functional groups, there are in principle a number of possibilities. Since virtually all the chemical functionalities of Cml (Fig. 1) are known to contribute to its effectiveness as an inhibitor of ribosomal peptidyltransferase activity (15, 33), it is not surprising that there have been reports of enzyme-mediated resistance to Cml arising from dehalogenation, nitro group reduction, and hydrolysis of the amide bond (for a review, see reference 36) and modification of one or both of the hydroxyls of Cml by phosphorylation (26) and acetylation (36–38). Nonetheless, after more than four decades of medical and veterinary use, the preponderant enzymatic modification mechanism that has been observed to underlie Cml resistance in bacteria of clinical importance is that of O-acetylation.

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