AI Article Synopsis
- A terpene synthase (LcTPS2) was isolated from the plant Leucosceptrum canum, capable of producing unique macrocyclic terpenoids.
- Engineered versions of bacteria and plants were able to produce six new types of sesterterpenoids, marking a significant advancement in terpenoid research with the largest ring system identified so far.
- Certain engineered variants of LcTPS2 showed increased production of these compounds and demonstrated the ability to inhibit T-cell production, offering potential applications in biocatalysis and plant biosynthesis.
Article Abstract
A versatile terpene synthase (LcTPS2) producing unconventional macrocyclic terpenoids was characterized from Leucosceptrum canum. Engineered Escherichia coli and Nicotiana benthamiana expressing LcTPS2 produced six 18-/14-membered sesterterpenoids including five new ones and two 14-membered diterpenoids. These products represent the first macrocyclic sesterterpenoids from plants and the largest sesterterpenoid ring system identified to date. Two variants F516A and F516G producing approximately 3.3- and 2.5-fold, respectively, more sesterterpenoids than the wild-type enzyme were engineered. Both 18- and 14-membered ring sesterterpenoids displayed significant inhibitory activity on the IL-2 and IFN-γ production of T cells probably via inhibition of the MAPK pathway. The findings will contribute to the development of efficient biocatalysts to create bioactive macrocyclic sesterterpenoids, and also herald a new potential in the well-trodden territory of plant terpenoid biosynthesis.
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| http://dx.doi.org/10.1002/anie.202110842 | DOI Listing |
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