Reinvestigation of the Mechanism and Selectivity of 1,8-Cineole Synthase using TerDockin

Abstract

The mechanism of 1,8-cineole formation in Streptomyces clavuligerus 1,8-cineole synthase was reinvestigated using the TerDockin modeling approach and compared to that in Salvia fruticosa. The results of these simulations provided new data on the binding modes of carbocations, the nature of active site bases, and enantioselectivity. In particular, the likelihood of pathways involving R and S terpinyl cation were assessed, and differentiation of these was found to relate to the position of active site bases rather than selective binding of the carbocations.