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.[1]References
- Puromycin analogues. Effect of aryl-substituted puromycin analogues on the ribosomal peptidyltransferase reaction. Lee, H., Fong, K.L., Vince, R. J. Med. Chem. (1981) [Pubmed]
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