Chloramphenicol Acetylation in Streptomyces

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Abstract
Actinomycete strains (21) [Nocardia mediterranei, Streptomyces sp., S. coelicolor, S. acrimycini, S. lividans, S. glaucescens, S. rimosus, S. roseochromogenes, S. viridochromogenes, S. venezuelae, S. venezuelae var. spiralis, S. erythrochromogenes and S. griseus] were screened for the presence of chloramphenicol acetyltransferase, the enzyme responsible for chloramphenicol resistance in many species of bacteria. Only 5 strains belonging to 3 spp. yielded mycelial lysates which catalyzed the formation of chloramphenicol acetates in the presence of acetyl-coA: S. coelicolor Mueller, S. acrimycini and S. griseus. A mutant of S. acrimycini selected for an increase in resistance to chloramphenicol had a higher specific activity for chloramphenicol acetyltransferase than that in the parental strain; the enzyme was not inducible in the mutant, the parental strain or any other strain tested. Chloramphenicol was not acetylated by lysates of a strain of S. venezuelae, the producer organism.