Sulfoxide configuration in sparsomycin determines time-dependent and competitive inhibition of peptidyl transferase

Ash, R.J., Flynn, G.A., Liskamp, R.M. and Ottenheijm, H.C. (1984) Sulfoxide configuration in sparsomycin determines time-dependent and competitive inhibition of peptidyl transferase. Biochemical and Biophysical Research Communications, 125(2), pp. 784-789. (doi:10.1016/0006-291X(84)90607-7)

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Abstract

Sparsomycin, ScRs configuration, was the most potent of the four possible stereoisomers as a competitive inhibitor of peptide bond formation. In addition, the configuration of the two chiral centers dictated whether the compound exhibited time- and temperature-dependent inhibition of peptidyl transferase when incubated with polysomes prior to enzyme assay. The data corroborate the thesis that a peptidyl transferase-mediated acylation of the pivotal sulfoxide moiety and subsequent Pummerer rearrangement play a significant role in the inhibitory properties of sparsomycin.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Ash, R.J., Flynn, G.A., Liskamp, R.M., and Ottenheijm, H.C.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biochemical and Biophysical Research Communications
ISSN:0006-291X
ISSN (Online):1090-2104

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