ArticleChembiochem : a European journal of chemical biology2020
Taming the Reactivity of Monoterpene Synthases To Guide Regioselective Product Hydroxylation.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed.
- Reinvestigation of the mechanism and selectivity of 1,8-cineole synthase usingChemical science · 2026Article
- Expanding the substrate scope of a bacterial monoterpene synthase for the production of sesquiterpenoid and diterpenoid products.The FEBS journal · 2026Article
- Mechanistic Insights into GTP Hydrolysis by the RhoA Protein: Catalytic Impact of Glutamine Tautomerism.ACS catalysis · 2025Article
- Differential Substrate Sensing in Terpene Synthases from Plants and Microorganisms: Insight from Structural, Bioinformatic, and EnzyDock Analyses.Angewandte Chemie (International ed. in English) · 2024Article
- Regiodivergent Radical Termination for Intermolecular Biocatalytic C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- Decoding Catalysis by Terpene Synthases.ACS catalysis · 2023Review
- Structural Understanding of Fungal Terpene Synthases for the Formation of Linear or Cyclic Terpene Products.ACS catalysis · 2023Article
- How a 10-ACS catalysis · 2022Article
- Molecular Determinants of Carbocation Cyclisation in Bacterial Monoterpene Synthases.Chembiochem : a European journal of chemical biology · 2022Article
- Predictive Engineering of Class I Terpene Synthases Using Experimental and Computational Approaches.Chembiochem : a European journal of chemical biology · 2022Review
- Redesigning the Molecular Choreography to Prevent Hydroxylation in Germacradien-11-ol Synthase Catalysis.ACS catalysis · 2021Article
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Taming the Reactivity of Monoterpene Synthases To Guide Regioselective Product Hydroxylation.Chembiochem : a European journal of chemical biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Monoterpenoids are industrially important natural products with applications in the flavours, fragrances, fuels and pharmaceutical industries. Most monoterpenoids are produced by plants, but recently two bacterial monoterpene synthases have been identified, including a cineole synthase (bCinS). Unlike plant cineole synthases, bCinS is capable of producing nearly pure cineole from geranyl diphosphate in a complex cyclisation cascade that is tightly controlled. Here we have used a multidisciplinary approach to show that Asn305 controls water attack on the α-terpinyl cation and subsequent cyclisation and deprotonation of the α-terpineol intermediate, key steps in the cyclisation cascade which direct product formation towards cineole. Mutation of Asn305 results in variants that no longer produce α-terpineol or cineole. Molecular dynamics simulations revealed that water coordination is disrupted in all variants tested. Quantum mechanics calculations indicate that Asn305 is most likely a (transient) proton acceptor for the final deprotonation step. Our synergistic approach gives unique insight into how a single residue, Asn305, tames the promiscuous chemistry of monoterpene synthase cyclisation cascades. It does this by tightly controlling the final steps in cineole formation catalysed by bCinS to form a single hydroxylated monoterpene product.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.