Structure-guided product determination of the bacterial type II diterpene synthase Tpn2

Abstract

Crystal structure elucidation of terpene synthases plays an important role to understand the sequence-structure-function relationships of this enzyme class. Here, the authors determine the crystal structure of bacterial terpene synthase Tpn2, probe the catalytic mechanism by structure-guided mutation, and change the product preference from a clerodane skeleton to a syn-labdane skeleton.