| Autor: |
Lan Jiang, Kangjie Lv, Guoliang Zhu, Zhi Lin, Xue Zhang, Cuiping Xing, Huanting Yang, Weiyan Zhang, Zhixin Wang, Chengwei Liu, Xudong Qu, Tom Hsiang, Lixin Zhang, Xueting Liu |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Synthetic and Systems Biotechnology, Vol 7, Iss 4, Pp 1142-1147 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2405-805X |
| DOI: |
10.1016/j.synbio.2022.08.002 |
| Popis: |
The chemical diversity of terpenoids is typically established by terpene synthase-catalyzed cyclization and diversified by post-tailoring modifications. Fungal bifunctional terpene synthase (BFTS) associated P450 enzymes have shown significant catalytic potentials through the development of various new terpenoids with different biological activities. This study discovered the BFTS and its related gene cluster from the plant endophytic fungus Didymosphaeria variabile 17020. Heterologous expression of the BFTS in Saccharomyces cerevisiae resulted in the characterization of a major product diterpene variediene (1), along with two new minor products neovariediene and neoflexibilene. Further heterologous expression of the BFTS and one cytochrome P450 enzyme VndE (CYP6138B1) in Aspergillus oryzae NSAR1 led to the identification of seven norditerpenoids (19 carbons) with a structurally unique 5/5 bicyclic ring system. Interestingly, in vivo experiments suggested that the cyclized terpene variediene (1) was modified by VndE along with the endogenous enzymes from the host cell A. oryzae through serial chemical conversions, followed by multi-site hydroxylation via A. oryzae endogenous enzymes. Our work revealed that the two-enzymes biosynthetic system and host cell machinery could produce structurally unique terpenoids. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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