ArticleJournal of the American Chemical Society2019
Thiopeptide Pyridine Synthase TbtD Catalyzes an Intermolecular Formal Aza-Diels-Alder Reaction.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Enzymatic Pyridine Aromatization during Thiopeptide Biosynthesis.Journal of the American Chemical Society · 2022Article
- Synthesis of Stereoenriched Piperidines via Chemo-Enzymatic Dearomatization of Activated Pyridines.Journal of the American Chemical Society · 2022Article
- Antifungal activity and genomic characterization of the biocontrol agent Bacillus velezensis CMRP 4489.Scientific reports · 2022Article
- Accessing Diverse Pyridine-Based Macrocyclic Peptides by a Two-Site Recognition Pathway.Journal of the American Chemical Society · 2022Article
- Byproduct formation during the biosynthesis of spinosyn A and evidence for an enzymatic interplay to prevent its formation.Tetrahedron · 2022Article
- Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Challenges and advances in genome mining of ribosomally synthesized and post-translationally modified peptides (RiPPs).Synthetic and systems biotechnology · 2020Review
- Interception of the Bycroft-Gowland Intermediate in the Enzymatic Macrocyclization of Thiopeptides.Journal of the American Chemical Society · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Thiopeptide pyridine synthases catalyze a multistep reaction involving a unique and nonspontaneous intramolecular aza-[4 + 2] cycloaddition between two dehydroalanines to forge a trisubstituted pyridine core. We discovered that the in vitro activity of pyridine synthases from the thiocillin and thiomuracin pathways are significantly enhanced by general base catalysis and that this broadly expands the enzymes substrate tolerance. Remarkably, TbtD is competent to perform an intermolecular cyclization in addition to its cognate intramolecular reaction, underscoring its versatility as a biocatalyst. These data provide evidence that pyridine synthases use a two-site substrate recognition model to engage and process their substrates.
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