Structure and evolution guided investigations of terpene synthase mechanism (769.11)

Abstract

Structure and evolution guided investigations of terpene synthase mechanism Reuben J. Peters Department of Biochem., Biophys. & Mol. Biol., Iowa State University Terpene synthases catalyze wonderfully complex reactions, involving cyclization and/or rearrangements of isoprenyl diphosphate precursors. These reactions are driven by carbocationic cascades, which can be initiated in two distinct ways. Class I terpene synthases catalyze heterolytic cleavage of an allylic diphosphate ester bond to initiate their reactions, while class II terpene synthases utilize protonation for the same purpose. Building on our recent determination of high‐resolution crystal structures for both classes of terpene synthases, along with the conservation pattern underlying the evolution of novel function, we are probing the underlying enzymatic structure‐function relationships. Our results have revealed the ability of single residues changes to dramatically remodel reaction outcome, highlighting the role of electrostatic effects and providing significant insights into the catalyzed complex reactions.Grant Funding Source: GM076324