Penicillin biosynthesis: active substrates derived by methoxy substitution in the valinyl residue of the natural substrate
Abstract
The structure–reactivity profile of tripeptides modified by methoxy substitution in the valinyl moiety of L-(α-aminoadipoyl)-L-cysteinyl-D-valine with the enzyme isopenicillin N synthase has been examined; substrate bulk and absolute configuration at the oxygen-substituted carbon were found to play crucial roles in determining substrate reactivity.