ArticleNature catalysis2021
Catalytic mechanism and
Article in Nature catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- An Antifungal with a Novel Mechanism of Action Discovered via Resistance Gene-Guided Genome Mining.ACS central science · 2026Article
- The Diels-Alder Reaction as a Key Step in Natural Product Synthesis.Progress in the chemistry of organic natural products · 2026Review
- Resistance Gene-Guided Discovery of a Fungal Spirotetramate as an Acetolactate Synthase Inhibitor.Journal of the American Chemical Society · 2025Article
- Catalyst-controlled regiodivergence and stereodivergence in formal cross-[4+2] cycloadditions: The unique effect of bismuth(III).Science advances · 2025Article
- Iminium Catalysis in Natural Diels-Alderase.Nature catalysis · 2025Article
- Biocatalyzed and Photochemical Formal [2+2] Cycloaddition of Euphoboetirane A: A Route to a Fused Pentacyclic Diterpene Skeleton.Organic letters · 2025Article
- Non-enzymatic reactions in biogenesis of fungal natural products.Journal of natural medicines · 2024Review
- Valence-isomer selective cycloaddition reaction of cycloheptatrienes-norcaradienes.Nature communications · 2024Article
- Tandem intermolecular [4 + 2] cycloadditions are catalysed by glycosylated enzymes for natural product biosynthesis.Nature chemistry · 2023Article
- Biosynthesis of Polycyclic Natural Products from Conjugated Polyenes via Tandem Isomerization and Pericyclic Reactions.Journal of the American Chemical Society · 2023Article
- EnzymaticJournal of the American Chemical Society · 2023Article
- Deciphering chemical logic of fungal natural product biosynthesis through heterologous expression and genome mining.Natural product reports · 2023Review
- cis-Decalin-containing tetramic acids as inhibitors of insect steroidogenic glutathione S-transferase Noppera-bo.PloS one · 2023Article
- Pericyclases for cycloaddition.National science review · 2022Article
- Combining iminium and supramolecular catalysis for the [4 + 2] cycloaddition ofOrganic & biomolecular chemistry · 2022Article
- Engineered P450 Atom-Transfer Radical Cyclases are Bifunctional Biocatalysts: Reaction Mechanism and Origin of Enantioselectivity.Journal of the American Chemical Society · 2022Article
- Discovery and characterization of a terpene biosynthetic pathway featuring a norbornene-forming Diels-Alderase.Nature communications · 2022Article
- Recent advances in the chemo-biological characterization of decalin natural products and unraveling of the workings of Diels-Alderases.Fungal biology and biotechnology · 2022Review
- New Trends and Future Opportunities in the Enzymatic Formation of C-C, C-N, and C-O bonds.Chembiochem : a European journal of chemical biology · 2022Review
- Redesigning Enzymes for Biocatalysis: Exploiting Structural Understanding for Improved Selectivity.Frontiers in molecular biosciences · 2022Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
We have previously reported the identification of CghA, a proposed Diels-Alderase responsible for the formation of the bicyclic octalin core of the fungal secondary metabolite Sch210972. Here we show the crystal structure of the CghA-product complex at a resolution of 2.0 Å. Our result provides the second structural determination of eukaryotic Diels-Alderases and adds yet another fold to the family of proteins reported to catalyse [4 + 2] cycloaddition reactions. Site-directed mutagenesis-coupled kinetic characterization and computational analyses allowed us to identify key catalytic residues and propose a possible catalytic mechanism. Most interestingly, we were able to rationally engineer CghA such that the mutant was able to catalyse preferentially the formation of the energetically disfavoured
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.