Peptidyl transferase substrate activity and inhibition of protein biosynthesis by a hydrophilic-aminoacyl analogue of puromycin

• Published in: Biochemical and biophysical research communications Vol. 81; no. 2; pp. 559 - 564
• Main Authors: Vince, Robert, Fong, Kei-Lai L.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.03.1978
• Subjects: Acyltransferases - metabolism; Escherichia coli - metabolism; Kinetics; Peptidyl Transferases - metabolism; Protein Biosynthesis - drug effects; Puromycin - analogs & derivatives; Puromycin - pharmacology; Ribosomes - metabolism; RNA, Transfer - metabolism

A puromycin analogue possessing a hydrophilic amino acid, 3′-N-[S-(6-hydroxyhexyl)- L -cysteinyl]puromycin aminonucleoside, has been prepared and examined as a substrate for ribosomal peptidyl transferase. Kinetic studies indicate that this non-aromatic aminoacyl analogue is 95.6% as efficient as th...