ArticleThe FEBS journal2017
Characterization of the first naturally thermostable terpene synthases and development of strategies to improve thermostability in this family of enzymes.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Optimization of IspSApplied and environmental microbiology · 2023Article
- Protein engineering strategies for microbial production of isoprenoids.Metabolic engineering communications · 2020Review
- Protein Engineering for Improving and Diversifying Natural Product Biosynthesis.Trends in biotechnology · 2020Review
- Exploring novel bacterial terpene synthases.PloS one · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The terpenoid family of natural products is being targeted for heterologous microbial production as a cheaper and more reliable alternative to extraction from plants. The key enzyme responsible for diversification of terpene structure is the class-I terpene synthase (TS), and these often require engineering to improve properties such as thermostability, robustness and catalytic activity before they are suitable for industrial use. Improving thermostability typically relies on screening a large number of mutants, as there are no naturally thermostable TSs described upon which to base rational design decisions. We have characterized the first examples of natural TSs exhibiting thermostability, which catalyse the formation of the sesquiterpene τ-muurolol at temperatures up to 78 °C. We also report an enzyme with a k DATABASE: Model data are available in the PMDB database under the accession number PM0080780.
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