Mechanistic Investigations on Microbial Type I Terpene Synthases through Site-Directed Mutagenesis

Abstract

AbstractDuring the past three decades many terpene synthases have been characterised from all kingdoms of life. Enzymes of type I, from bacteria, fungi and protists, commonly exhibit several highly conserved motifs and single residues, and the available crystal structures show a shared α-helical fold, while the overall sequence identity is generally low. Several enzymes have been studied by site-directed mutagenesis, giving valuable insights into terpene synthase catalysis and the intriguing mechanisms of terpene synthases. Some mutants are also preparatively useful and give higher yields than the wild type or a different product that is otherwise difficult to access. The accumulated knowledge obtained from these studies is presented and discussed in this review.1 Introduction2 Residues for Substrate Binding and Catalysis3 Residues with Structural Function4 Residues Contouring the Active Site Cavity5 Other Residues6 Conclusions