ArticleAngewandte Chemie (International ed. in English)2023
Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Mechanistic Characterisation of Bacterial Terpene Synthases from Chitinophagaceae Producing Marine-Type Diterpenes.Angewandte Chemie (International ed. in English) · 2025Article
- Exploring and expanding the natural chemical space of bacterial diterpenes.Nature communications · 2025Article
- From Monocyclization to Pentacyclization: A Versatile Plant Cyclase Produces Diverse Sesterterpenes with Anti-Liver Fibrosis Potential.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Mechanistic Characterisation and Engineering of Sesterviolene Synthase from Streptomyces violens.Angewandte Chemie (International ed. in English) · 2023Article
- Functional characterisation of twelve terpene synthases from actinobacteria.Beilstein journal of organic chemistry · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sesterviolene synthase from Streptomyces violens was identified and represents the second known sesterterpene synthase from bacteria. Isotopic labelling experiments in conjunction with DFT calculations were performed that provided detailed insight into its complex cyclisation mechanism. Enzyme engineering through site-directed mutagenesis gave access to a high-yielding enzyme variant that provided six additional minor products and the main product in sufficient quantities to study its chemistry.
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Registered trials
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