Abstract
A detailed kinetic study was carried out on the inhibitory mechanisms of two eukaryotic peptidyltransferase drugs (I), anisomycin and sparsomycin. In an in vitro system from rabbit reticulocytes, AcPhe-puromycin is produced in a pseudo-first-order reaction from the preformed AcPhe-tRNA/poly(U)/80S ribosome complex (complex C) and excess puromycin (S). This reaction is inhibited by anisomycin and sparsomycin through different mechanisms. Anisomycin acts as a mixed noncompetitive inhibitor. The product, AcPhe-puromycin, is derived only from C according to the puromycin reaction. On the other hand, sparsomycin reacts with complex C in a two-step reaction,
Footnotes
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Send reprint requests to: Dr. Dennis Synetos, Laboratory of Biochemistry, School of Medicine, University of Patras, Greece. E-mail:dsynetos{at}med.upatras.gr
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This work was supported in part by a grant from the General Secretariat of Research and Technology, Ministry of Development of Greece.
- Received December 15, 1997.
- Accepted February 10, 1998.
- The American Society for Pharmacology and Experimental Therapeutics
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