Structure Model‐Guided Reprogramming Enables Functional Interconversion of Phomactatriene and Verticillene Synthases

L Li Zhang Y Yinghan Chen (State Key Laboratory of Analytical Chemistry for Life Science, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering) Y Yan Wang A Ao Zhu (State Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences) Y Yi Ling Hu (State Key Laboratory of Pharmaceutical Biotechnology Institute of Functional Biomolecules Department of Neurology Nanjing Drum Tower Hospital Chemistry and Biomedicine Innovation Center (ChemBIC) School of Life Sciences Nanjing University Nanjing 210023 China) X Xiao Ling Huang (State Key Laboratory of Pharmaceutical Biotechnology, Institute of Functional Biomolecules, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences Nanjing University Nanjing 210023 China) Q Qi Zhang Y Yong Liang J Jing Shi H Hui Ming Ge (State Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences)

Abstract

Abstract Terpenoids represent the most structurally diverse class of natural products on Earth. Terpene synthases are key enzymes for constructing the complex and varied terpene skeletons by catalyzing the formation of multiple carbon–carbon bonds. Phomactatriene and verticillene family natural products are both classified as bicyclic diterpenoids, sharing a unique bicyclo[9.3.1]pentadecane skeleton. In this study, we used genome mining to identify the phomactatriene synthase SiPS from bacteria, together with two verticillene synthases, LxVS and AxVS. Our DFT calculations revealed that the rearrangement pathways for compounds in the phomactatriene and verticillene families follow a shared biosynthetic route. Furthermore, through comparative structural model analyses of the phomactatriene and verticillene synthases, we employed molecular modelling and site‐directed mutagenesis to facilitate functional interconversion between these distinct terpene synthases. This work enhances our understanding of terpene biosynthesis and the potential for engineering terpene synthases for biotechnological applications.

Article Details

Volume / Issue Vol. 64, Issue 52
Published December 22, 2025
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (10)

L

Li Zhang

Y

Yinghan Chen

State Key Laboratory of Analytical Chemistry for Life Science, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering

Y

Yan Wang

A

Ao Zhu

State Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences

Y

Yi Ling Hu

State Key Laboratory of Pharmaceutical Biotechnology Institute of Functional Biomolecules Department of Neurology Nanjing Drum Tower Hospital Chemistry and Biomedicine Innovation Center (ChemBIC) School of Life Sciences Nanjing University Nanjing 210023 China

X

Xiao Ling Huang

State Key Laboratory of Pharmaceutical Biotechnology, Institute of Functional Biomolecules, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences Nanjing University Nanjing 210023 China

Q

Qi Zhang

Y

Yong Liang

J

Jing Shi

H

Hui Ming Ge

State Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Nanjing Drum Tower Hospital, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences