Abstract
During 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 Introduction
2 Residues for Substrate Binding and Catalysis
3 Residues with Structural Function
4 Residues Contouring the Active Site Cavity
5 Other Residues
6 Conclusions
Key words
terpenes - biosynthesis - mutagenesis - enzyme mechanisms