Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from .
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| Autores principales: | , , , , , |
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| Formato: | Artículo científico |
| Lenguaje: | en |
| Publicado: |
Molecules (Basel, Switzerland)
2026
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| _version_ | 1868266053577998337 |
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| author | He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu |
| author_facet | He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu |
| collection | PubMed - marine biology |
| contents | Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from . He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu Alkyl and Aryl Transferases Diterpenes Mutagenesis Plant Proteins Transcriptome Over the past decade, an increasing number of functional microbial-like terpene synthases (MTPSLs) have been reported in non-seed plants. However, whether the traditional Chinese medicinal plant harbors such enzymes and their corresponding functions remains unexplored. In this study, we mined the transcriptome of and identified a microbial-like terpene synthase, MTPSL1, which produces multiple diterpene products. Following isolation and structural elucidation, seven distinct compounds were obtained, representing three skeletal types: spatane, prenylkelsoene-type, and biflorane. Among these, compound is a novel biflorane diterpene. Structural analysis and subsequent mutagenesis revealed critical residues governing the formation of distinct skeletons, uncovering the multifunctional nature of this enzyme. Notably, the S224A mutation significantly enhanced the production of spatane diterpene compound by 11.6-fold, demonstrating the potential for protein engineering to improve the yield of this bioactive marine-specific diterpene. Transcriptomic profiling revealed that MTPSL1 is highly expressed in sporangia, and co-expression analysis with cytochrome P450s identified the CYP781 subfamily as candidates potentially involved in the downstream modification of these skeletons. Collectively, we report the first MTPSL from and characterize it as a multifunctional diterpene synthase. Through structure-guided mutagenesis, we uncovered the molecular basis of its functional versatility, with the S224A mutation providing a powerful tool for enhancing the yields of all three diterpene skeletons, thereby laying a foundation for future protein engineering and synthetic biology applications. |
| format | Artículo científico |
| id | pubmed_42076007 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Molecules (Basel, Switzerland) |
| record_format | pubmed |
| spellingShingle | Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from . He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu Alkyl and Aryl Transferases Diterpenes Mutagenesis Plant Proteins Transcriptome Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from . He, Ting Zhao, Yao Li, Xin Chen, Bao Chen, Fangyan Xu, Baofu Alkyl and Aryl Transferases Diterpenes Mutagenesis Plant Proteins Transcriptome Over the past decade, an increasing number of functional microbial-like terpene synthases (MTPSLs) have been reported in non-seed plants. However, whether the traditional Chinese medicinal plant harbors such enzymes and their corresponding functions remains unexplored. In this study, we mined the transcriptome of and identified a microbial-like terpene synthase, MTPSL1, which produces multiple diterpene products. Following isolation and structural elucidation, seven distinct compounds were obtained, representing three skeletal types: spatane, prenylkelsoene-type, and biflorane. Among these, compound is a novel biflorane diterpene. Structural analysis and subsequent mutagenesis revealed critical residues governing the formation of distinct skeletons, uncovering the multifunctional nature of this enzyme. Notably, the S224A mutation significantly enhanced the production of spatane diterpene compound by 11.6-fold, demonstrating the potential for protein engineering to improve the yield of this bioactive marine-specific diterpene. Transcriptomic profiling revealed that MTPSL1 is highly expressed in sporangia, and co-expression analysis with cytochrome P450s identified the CYP781 subfamily as candidates potentially involved in the downstream modification of these skeletons. Collectively, we report the first MTPSL from and characterize it as a multifunctional diterpene synthase. Through structure-guided mutagenesis, we uncovered the molecular basis of its functional versatility, with the S224A mutation providing a powerful tool for enhancing the yields of all three diterpene skeletons, thereby laying a foundation for future protein engineering and synthetic biology applications. |
| title | Functional Characterization and Mutagenesis Studies of a Microbial-like Diterpene Synthase from . |
| topic | Alkyl and Aryl Transferases Diterpenes Mutagenesis Plant Proteins Transcriptome |
| url | https://pubmed.ncbi.nlm.nih.gov/42076007/ |