Genome Mining of Terpene Synthases from Fourteen <i>Streptomyces</i> Strains
Terpenoids are the most structurally diverse class of natural products (NPs). Despite their abundance, the functional diversity of bacterial terpene synthases (TPSs), particularly from <i>Streptomyces</i> species, remains largely unexplored. In this study, fourteen <i>Streptomyces&...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-06-01
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| Series: | Microorganisms |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2076-2607/13/7/1479 |
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| Summary: | Terpenoids are the most structurally diverse class of natural products (NPs). Despite their abundance, the functional diversity of bacterial terpene synthases (TPSs), particularly from <i>Streptomyces</i> species, remains largely unexplored. In this study, fourteen <i>Streptomyces</i> strains were subjected to genome sequencing and bioinformatic analysis to systematically mine class I TPSs. A total of forty-eight TPSs were identified and categorized through phylogenetic analysis, and five representative TPSs distantly related to known TPSs were selected for functional investigation. Biochemical assays revealed that TAC28_6116 is a sesquiterpene synthase producing thujopsan-2β-ol (<b>1</b>) and thujopsene (<b>2</b>), marking the first report of thujopsan-2β-ol production from a bacterial source. TAC49_7078 is a diterpene synthase responsible for the formation of <i>ent</i>-phomacta-1(15),3,7-triene (<b>3</b>). Notably, TAC43_2999 was identified as a novel sesterterpene synthase that produced compound <b>5</b> in vitro, while the generation of a previously undescribed compound <b>6</b>, sestermalaysiene, was exclusively detected during in vivo fermentation using the engineered <i>Escherichia coli</i> chassis optimized for terpenoid biosynthesis. Structural elucidation of sestermalaysiene was supported by nuclear magnetic resonance (NMR) analysis and quantum chemical calculations. Its formation might proceed via a rare [4 + 2] cycloaddition mechanism. Overall, this work expands our knowledge of the catalytic diversity of bacterial TPSs and offers promising biocatalysts for terpenoid engineering and discovery. |
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| ISSN: | 2076-2607 |