Puromycin analogues. Effect of aryl-substituted puromycin analogues on the ribosomal peptidyltransferase reaction.
A series of ortho- and para-substituted L-phenylalanylpuromycin analogues 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 greater than p-NHCOCH3 greater than p-NO2 = p-NHCO(CH2)2CH3 greater than p-NHCOCH2Br. However, the inability of the ribosome to tolerate a nitro group at the ortho position of the phenylalanine ring precluded the use of the photosensitive puromycin analogue, 2-nitro-4-azidophenylalanylpuromycin aminonucleoside (7a), as a photoaffinity label for the peptidyltransferase site.
D000217:Acyltransferases / Q000378:metabolism*; D001665:Binding Sites; D007700:Kinetics; D010458:Peptidyl Transferases / Q000378:metabolism*; D011691:Puromycin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D012270:Ribosomes / Q000201:enzymology*; D013329:Structure-Activity Relationship
D011691:Puromycin; D000217:Acyltransferases; D010458:Peptidyl Transferases