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

The relationship between the effect of different turimycin components on ribosomal peptidyltransferase of E. coli, antimicrobial activity and chemical structure were studied. Inhibition of peptidyltransferase as well as 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.