ArticleNature catalysis2019
Unexpected enzyme-catalysed [4+2] cycloaddition and rearrangement in polyether antibiotic biosynthesis.
Article in Nature catalysis, 2019. 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
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Who cites it
13 citing papers in PubMed.
- An enzymatic dual-oxa Diels-Alder reaction constructs the oxygen-bridged tricyclic acetal unit of (-)-anthrabenzoxocinone.Nature chemistry · 2025Article
- A metabologenomics strategy for rapid discovery of polyketides derived from modular polyketide synthases.Chemical science · 2025Article
- Interrogation of an Enzyme Library Reveals the Catalytic Plasticity of Naturally Evolved [4+2] Cyclases.Chembiochem : a European journal of chemical biology · 2023Article
- Catalytic asymmetric oxa-Diels-Alder reaction of acroleins with simple alkenes.Nature communications · 2023Article
- Discovery and characterization of a terpene biosynthetic pathway featuring a norbornene-forming Diels-Alderase.Nature communications · 2022Article
- Molecular Basis for Two Stereoselective Diels-Alderases that Produce Decalin Skeletons*.Angewandte Chemie (International ed. in English) · 2021Article
- Exo-selective intermolecular Diels-Alder reaction by PyrI4 and AbnU on non-natural substrates.Communications chemistry · 2021Article
- Discovery and investigation of natural Diels-Alderases.Journal of natural medicines · 2021Review
- Thiopeptides: antibiotics with unique chemical structures and diverse biological activities.The Journal of antibiotics · 2021Review
- Catalytic mechanism andNature catalysis · 2021Article
- An enzymatic Alder-ene reaction.Nature · 2020Article
- Understand the Specific Regio- and Enantioselectivity of Fluostatin Conjugation in the Post-Biosynthesis.Biomolecules · 2020Article
- The biosynthetic pathway to tetromadurin (SF2487/A80577), a polyether tetronate antibiotic.PloS one · 2020Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Enzymes catalysing remarkable Diels-Alder-like [4+2] cyclisations have been previously implicated in the biosynthesis of spirotetronate and spirotetramate antibiotics. Biosynthesis of the polyether antibiotic tetronasin is not anticipated to require such steps, yet the tetronasin gene cluster encodes enzymes Tsn11 and Tsn15, homologous to authentic [4+2] cyclases. Here we show that deletion of Tsn11 led to accumulation of a late-stage intermediate, in which the two central rings of tetronasin, and four of its 12 asymmetric centres, remain unformed.
Identifiers
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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.