Sulfoxide configuration in sparsomycin determines time-dependent and competitive inhibition of peptidyl transferase
1984
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.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
13
References
6
Citations
NaN
KQI