Characterization of the first naturally thermostable terpene synthases and development of strategies to improve thermostability in this family of enzymes.

ABSTRACT: The terpenoid family of natural products is being targeted for heterologous microbial production as a cheaper and more reliable alternative to extraction from plants. The key enzyme responsible for diversification of terpene structure is the class-I terpene synthase (TS), and these often require engineering to improve properties such as thermostability, robustness and catalytic activity before they are suitable for industrial use. Improving thermostability typically relies on screening a large number of mutants, as there are no naturally thermostable TSs described upon which to base rational design decisions. We have characterized the first examples of natural TSs exhibiting thermostability, which catalyse the formation of the sesquiterpene τ-muurolol at temperatures up to 78 °C. We also r

SUBMITTER: Styles MQ 

PROVIDER: S-EPMC6849719 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature