Unraveling the function of a marine bacterial terpene synthase

August 8, 2025

Atomic-level understanding enables enzyme function engineering

A research team at the RIKEN CSRS has elucidated the three-dimensional structure of a drimenol synthase (AsDMS) derived from the marine bacterium Aquimarina spongiae, which possesses a unique domain architecture. Furthermore, by introducing site-specific mutations into AsDMS, the team successfully engineered a functional enzyme capable of producing terpenoids distinct from drimenol.

Terpenoids are a diverse group of natural compounds produced by plants and certain microorganisms. They have supported the development of civilization, health, and food culture through their applications in pharmaceuticals, industrial materials, perfumes, and essential oils. In this study, the team demonstrated crystallographic analyses of AsDMS, revealing its overall structure and the atomic-level interactions between the enzyme and its substrates. This enabled the identification of key amino acid residues involved in substrate binding and catalysis. Furthermore, the team created several AsDMS variants by introducing site-specific mutations into these residues. Functional analysis of these variants not only deepened the atomic-level understanding of the catalytic mechanism by which AsDMS produces drimenol, but also enabled the creation of engineered enzymes capable of synthesizing terpenoids distinct from drimenol. This approach is expected to lead to enhanced enzymatic reactions and the production of a broader variety of terpenoids.

 

Original article

Chemical Science　doi: 10.1039/D5SC04719F

K. Fujiyama, H. Takagi, N. N. Q. Vo, N. Morita, T. Nogawa, S. Takahashi,

"Structural Insights into a Bacterial Terpene Cyclase Fused with Haloacid Dehalogenase-like Phosphatase".

Contact

Shunji Takahashi
Unit Leader
Natural Product Biosynthesis Research Unit