ArticleJournal of the American Chemical Society2015
Chemoenzymatic synthesis of thiazolyl peptide natural products featuring an enzyme-catalyzed formal [4 + 2] cycloaddition.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides.Journal of the American Chemical Society · 2024Article
- Rapid Peptide Cyclization Inspired by the Modular Logic of Nonribosomal Peptide Synthetases.Journal of the American Chemical Society · 2024Article
- A Compact Reprogrammed Genetic Code for De Novo Discovery of Proteolytically Stable Thiopeptides.Journal of the American Chemical Society · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Biosynthesis of Polycyclic Natural Products from Conjugated Polyenes via Tandem Isomerization and Pericyclic Reactions.Journal of the American Chemical Society · 2023Article
- Advances on the biosynthesis of pyridine rings.Engineering microbiology · 2023Review
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Enzymatic Pyridine Aromatization during Thiopeptide Biosynthesis.Journal of the American Chemical Society · 2022Article
- Accessing Diverse Pyridine-Based Macrocyclic Peptides by a Two-Site Recognition Pathway.Journal of the American Chemical Society · 2022Article
- Article
- Structure Prediction and Synthesis of Pyridine-Based Macrocyclic Peptide Natural Products.Organic letters · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- An enzymatic Alder-ene reaction.Nature · 2020Article
- Nonspecific Heme-Binding Cyclase, AbmU, Catalyzes [4 + 2] Cycloaddition during Neoabyssomicin Biosynthesis.ACS omega · 2020Article
- Interception of the Bycroft-Gowland Intermediate in the Enzymatic Macrocyclization of Thiopeptides.Journal of the American Chemical Society · 2020Article
- Precursor peptide-targeted mining of more than one hundred thousand genomes expands the lanthipeptide natural product family.BMC genomics · 2020Article
- Minimal lactazole scaffold for in vitro thiopeptide bioengineering.Nature communications · 2020Article
- Enzyme evolution in fungal indole alkaloid biosynthesis.The FEBS journal · 2020Review
- The expanding world of biosynthetic pericyclases: cooperation of experiment and theory for discovery.Natural product reports · 2019Review
- Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019Review
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6 authors.
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Abstract
Thiocillins from Bacillus cereus ATCC 14579 are members of the well-known thiazolyl peptide class of natural product antibiotics, the biosynthesis of which has recently been shown to proceed via post-translational modification of ribosomally encoded precursor peptides. It has long been hypothesized that the final step of thiazolyl peptide biosynthesis involves a formal [4 + 2] cycloaddition between two dehydroalanines, a unique transformation that had eluded enzymatic characterization. Here we demonstrate that TclM, a single enzyme from the thiocillin biosynthetic pathway, catalyzes this transformation. To facilitate characterization of this new class of enzyme, we have developed a combined chemical and biological route to the complex peptide substrate, relying on chemical synthesis of a modified C-terminal fragment and coupling to a 38-residue leader peptide by means of native chemical ligation (NCL). This strategy, combined with active enzyme, provides a new chemoenzymatic route to this promising class of antibiotics.
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