Inhibition of protein biosynthesis: The first active sparsomycin analog

Robert Vince; Jay Brownell; Chang Kiu Lee

doi:10.1016/0006-291X(77)91509-1

Inhibition of protein biosynthesis: The first active sparsomycin analog

Robert Vince, Jay Brownell, Chang Kiu Lee

Center for Drug Design

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16 Scopus citations

Abstract

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)
Pages (from-to)	563-567
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	75
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(77)91509-1
State	Published - Apr 11 1977

Bibliographical note

Funding 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,

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abstract = "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.",

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AU - Brownell, Jay

AU - Kiu Lee, Chang

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AB - 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.

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Inhibition of protein biosynthesis: The first active sparsomycin analog

Abstract

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