Effect of the leucomycin-like macrolide antibiotic turimycin on ribosomal peptidyltransferase from Escherichia coli.

Abstract
The relationship between the effect of different turimycin components on ribosomal peptidyltransferase of E. coli, antimicrobial [antibacterial] activity and chemical structure were studied. Inhibition of peptidyltransferase and antimicrobial activity increased with the length of the aliphatic side chain in 4"-position of mycarose and decreased with acylation in 3-position of the lactone ring. Inhibition of peptidyltransferase is paralleled by inhibition of acceptor substrate binding.

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