A series of ortho-and para-substituted bphenyhylpuromycin analagues were synthesized and evaluated as substrates for the peptidyltransferase reaction of Escherichia coli ribosomes. Kinetic results reveal that substitution of the p-methoxy group of the puromycin molecule alters the peptidyltransferase activity of the molecule with the following decreasing order of substrate efficiencies: p-NH2> p-NHCOCHS> p-NOz= p-NHCO (CH&2HS> p- ...
