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Chimeric Terpene Synthases Possessing both Terpene Cyclization and Prenyltransfer Activities
Takaaki Mitsuhashi1, Ikuro Abe1
1Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Chembiochem : a European Journal of Chemical Biology
|April 21, 2018
Summary
Chimeric prenyltransferase (PT) and terpene synthase (TPS) enzymes, recently discovered in fungi, fuse two key roles in terpenoid biosynthesis. These unique enzymes are widely distributed and involved in producing diverse terpene natural products.
Area of Science:
- Biochemistry
- Natural Product Chemistry
- Mycology
Background:
- Terpenoids are diverse natural products synthesized via the prenyltransferase (PT) and terpene synthase (TPS) pathways.
- Typically, PTs and TPSs function as separate enzymes, controlling chain length and structural complexity, respectively.
- A novel chimeric enzyme, combining PT and TPS functions, was first identified in fungi in 2007.
Purpose of the Study:
- To review the current understanding of chimeric terpene synthases.
- To highlight their prevalence and significance in fungal secondary metabolism.
- To discuss their role in the biosynthesis of various terpenoids, including sesterterpenes.
Main Methods:
- Literature review of recent studies on fungal terpene synthases.
- Analysis of genomic and biochemical data on chimeric enzyme distribution.
- Examination of the functional roles of chimeric TPSs in natural product synthesis.
Main Results:
- Chimeric PT-TPS enzymes are widely distributed across fungal species.
- These enzymes play a crucial role in the biosynthesis of diverse terpenoids.
- They are particularly important in the formation of sesterterpenes, a rare class of terpenoids.
Conclusions:
- Chimeric terpene synthases represent a unique evolutionary adaptation in fungi.
- Their discovery has expanded our understanding of terpenoid biosynthesis pathways.
- Further research into these enzymes may uncover novel natural products and biosynthetic routes.
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