ArticleACS catalysis2024
From functional plasticity of two diterpene synthases (IrTPS2/IrKSL3a) to enzyme evolution.
Article in ACS catalysis, 2024. 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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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.
The trial behind it
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Who cites it
5 citing papers in PubMed.
- Engineered microorganisms unlock a new era of diterpenoid biomanufacturing: recent advances and future perspectives.Bioresources and bioprocessing · 2026Review
- Characterization and functional reconstruction of a highly productive germacrene A synthase from Liriodendron chinense.Plant biotechnology journal · 2025Article
- Dual distal insertions drive pimarane-to-miltiradiene rearrangement with enhanced enzymatic activity.Biodesign research · 2025Article
- Review
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
Terpenoids are an intriguing class of natural products with diverse structures and biological activities whose complexity stems, in large part, from terpene synthases (TPSs). These enzymes catalyze carbocationic cascade reactions wherein the groups responsible for quenching the final carbocation is generally not well known. IrKSL3a and IrTPS2 from
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Registered trials
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