ArticleNature chemistry2015
Substrate control in stereoselective lanthionine biosynthesis.
Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026Article
- Structure and Activity of Class II Lanthipeptides from a Thermophilic Bacterium.bioRxiv : the preprint server for biology · 2026Article
- An Unusual Ring Pattern in the Rosβ Lanthipeptide of the Two-Component Lantibiotic Roseocin.Journal of natural products · 2026Article
- Computational structure prediction of lanthipeptides with NMR data reveals underappreciated peptide flexibility.Protein science : a publication of the Protein Society · 2025Article
- A Unique Class of Cyclases with a Kinase Fold Catalyzes Enethiol-Mediated Macrocyclization of Aminovinyl-Cysteine Motifs in Lanthipeptides.ACS central science · 2025Article
- Decoding the Chemical Language of Ribosomally Synthesized and Post-Translationally Modified Peptides from the Untapped Archaea Domain.Angewandte Chemie (International ed. in English) · 2025Article
- Substrate prediction for RiPP biosynthetic enzymesDigital discovery · 2025Article
- Bibacillin 1: A two-component lantibiotic frombioRxiv : the preprint server for biology · 2024Article
- Article
- Expression and Subcellular Localization of Lanthipeptides in Human Cells.ACS synthetic biology · 2024Article
- Characterization of a LanC-free pathway for the formation of an ll-MeLan residue and anChemical science · 2024Article
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.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
- Substrate Prediction for RiPP Biosynthetic Enzymes via Masked Language Modeling and Transfer Learning.ArXiv · 2024Article
- Dehydroamino acid residues in bioactive natural products.Natural product reports · 2024Review
- Facile Method for Determining Lanthipeptide Stereochemistry.Analytical chemistry · 2024Article
- Hexagonal zinc oxide nanoparticles: a novel approach to combat multidrug-resistantFrontiers in cellular and infection microbiology · 2024Article
- Evidence of a Distinctive Enantioselective Binding Mode for the Photoinduced Radical Cyclization of α-Chloroamides in Ene-Reductases.ACS catalysis · 2023Article
- Benzylic Radical Stabilization Permits Ether Formation During Darobactin Biosynthesis.bioRxiv : the preprint server for biology · 2023Article
- Expression of Lanthipeptides in Human Cells.bioRxiv : the preprint server for biology · 2023Article
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4 authors.
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Abstract
Enzymes are typically highly stereoselective catalysts that enforce a reactive conformation on their native substrates. We report here a rare example in which the substrate controls the stereoselectivity of an enzyme-catalysed Michael-type addition during the biosynthesis of lanthipeptides. These natural products contain thioether crosslinks formed by a cysteine attack on dehydrated Ser and Thr residues. We demonstrate that several lanthionine synthetases catalyse highly selective anti-additions in which the substrate (and not the enzyme) determines whether the addition occurs from the re or si face. A single point mutation in the peptide substrate completely inverted the stereochemical outcome of the enzymatic modification. Quantum mechanical calculations reproduced the experimentally observed selectivity and suggest that conformational restraints imposed by the amino-acid sequence on the transition states determine the face selectivity of the Michael-type cyclization.
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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.