ArticleACS chemical biology2020
Structural Basis for Enzymatic Off-Loading of Hybrid Polyketides by Dieckmann Condensation.
Article in ACS chemical biology, 2020. 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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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Discovery and Biosynthetic Interrogation of a Cobalt-Containing Terpene-Polyketide-Nonribosomal Peptide Tribrid with Anticoronavirus Activity.Journal of the American Chemical Society · 2025Article
- Cryptic Cerulenin Rearrangement in Ketosynthase Covalent Inhibition.Journal of the American Chemical Society · 2024Article
- Mutagenetic analysis of the biosynthetic pathway of tetramate bripiodionen bearing 3-(2H-pyran-2-ylidene)pyrrolidine-2,4-dione skeleton.Microbial cell factories · 2024Article
- In Vitro Biochemical Characterization of Excised Macrocyclizing Thioesterase Domains from Non-ribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Biosynthetic Cyclization Catalysts for the Assembly of Peptide and Polyketide Natural Products.ChemCatChem · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
While several bioactive natural products that contain tetramate or pyridone heterocycles have been described, information on the enzymology underpinning these functionalities has been limited. Here we biochemically characterize an off-loading Dieckmann cyclase, NcmC, that installs the tetramate headgroup in nocamycin, a hybrid polyketide/nonribosomal peptide natural product. Crystal structures of the enzyme (1.6 Å) and its covalent complex with the epoxide cerulenin (1.6 Å) guide additional structure-based mutagenesis and product-profile analyses. Our results offer mechanistic insights into how the conserved thioesterase-like scaffold has been adapted to perform a new chemical reaction, namely, heterocyclization. Additional bioinformatics combined with docking and modeling identifies likely candidates for heterocycle formation in underexplored gene clusters and uncovers a modular basis of substrate recognition by the two subdomains of these Dieckmann cyclases.
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