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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