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

Li Zhang1, Yinghan Chen2, Yan Wang1

  • 1State 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.

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|October 29, 2025
PubMed
Summary
This summary is machine-generated.

Researchers identified bacterial terpene synthases for phomactatriene and verticillene, revealing a shared biosynthetic pathway. Engineering these enzymes offers potential for biotechnological applications in natural product synthesis.

Keywords:
Enzyme redesignMolecular dynamicsPhomactatrieneTerpene synthaseVerticillene

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Area of Science:

  • Natural Product Chemistry
  • Enzymology
  • Biotechnology

Background:

  • Terpenoids are the most structurally diverse natural products, synthesized by terpene synthases (TPS) that form complex carbon skeletons.
  • Phomactatriene and verticillene are bicyclic diterpenoids sharing a unique bicyclo[9.3.1]pentadecane skeleton.

Purpose of the Study:

  • To identify and characterize terpene synthases involved in the biosynthesis of phomactatriene and verticillene.
  • To elucidate the shared biosynthetic route and explore the potential for engineering terpene synthases.

Main Methods:

  • Genome mining was employed to identify bacterial terpene synthases: phomactatriene synthase (SiPS) and two verticillene synthases (LxVS, AxVS).
  • Density Functional Theory (DFT) calculations were used to analyze reaction pathways.
  • Comparative structural modeling, molecular modeling, and site-directed mutagenesis were performed to understand enzyme function and interconversion.

Main Results:

  • Identification of SiPS, LxVS, and AxVS, bacterial enzymes catalyzing the formation of phomactatriene and verticillene.
  • DFT calculations confirmed a shared biosynthetic pathway for both compound families.
  • Functional interconversion between distinct terpene synthases was achieved through structural analysis and mutagenesis.

Conclusions:

  • This study reveals a common biosynthetic origin for phomactatriene and verticillene families, mediated by specific terpene synthases.
  • The findings enhance understanding of terpene biosynthesis and enzyme evolution.
  • Engineering terpene synthases holds significant potential for biotechnological applications in producing diverse natural products.