A (dl) S-deoxo-S-propyl sparsomycin analog has been prepared and examined as an inhibitor of the peptidyl transferase reaction with bacterial ribosomes. A double reciprocal plot and Dixon analysis indicate that the sparsomycin analogy is a competitive inhibitor of phenylalanyl-puromycin formation. The inactivity of the L-isomer has established that the chiral carbon of sparsomycin analogs must be identical with the chirality of D-cysteinol for ribosomal binding.
|Original language||English (US)|
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Apr 11 1977|
Bibliographical noteFunding Information:
We wish to thank Dr. Paul F. Wiley, The Upjohn Company, for a sample of sparsomycin. This investigation was supported by Grants CA 13592 and CA 16623, and Research Career Development Award (to R.V.) CA 25258 from the National Cancer Institute,