Identification of new terpene synthases of marine bacterial origin

May 18, 2022

Production of new natural compounds

Researchers at the RIKEN CSRS searched bacterial protein databases for genes that encode enzymes involved in producing terpenoids and identified new sesquiterpene synthases of marine bacterial origin that catalyze the efficient production of drimenol (bicyclic drimane-type sesquiterpene) from farnesyl pyrophosphate (FPP).

There have been few practical applications of terpene synthases derived from bacteria. Therefore, it is significant to explore genes encoding new enzymes of bacterial origin and take advantage of them to produce useful compounds.

In this study, the researchers performed protein structure modeling of the drimenol synthase (DMS) derived from a marine bacterium Aquimarina spongiae (AsDMS). Then they carried out site-directed mutagenesis to identify a new drimenol synthase having functional domains completely different from those of other terpene synthases found in a wide range of plants. AsDMS has a novel structure consisting of a haloacid dehalogenase (HAD)-like hydrolase domain and a terpene synthase β domain, which evolved from different enzymatic origins. Further discovery and application of new terpene synthases are expected to be achieved.

These findings would facilitate the efficient production of terpenoids that are difficult to synthesize due to their complex structures and help create natural compounds with new bioactivities.

Original article: ACS Chemical Biology doi:10.1021/acschembio.2c00163; N. N. Q. Vo, T. Nomura, k. Kinugasa, H. Takagi, S. Takahashi,; "Identification and Characterization of Bifunctional Drimenol Synthases of Marine Bacterial Origin".
Contact: Shunji Takahashi; Unit Leader; Nhu Ngoc Quynh Vo; Postdoctoral Researcher