ArticleChemical communications (Cambridge, England)2017
Bypassing the proline/thiazoline requirement of the macrocyclase PatG.
Article in Chemical communications (Cambridge, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Chemoenzymatic tandem cyclization for the facile synthesis of bicyclic peptides.Communications chemistry · 2024Article
- Cheminformatics-Guided Cell-Free Exploration of Peptide Natural Products.Journal of the American Chemical Society · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Exploring the Limits of Cyanobactin Macrocyclase PatGmac: Cyclization of PawS-Derived Peptide Sunflower Trypsin Inhibitor-1 and Cyclotide Kalata B1.Journal of natural products · 2023Article
- Possible Functional Roles of Patellamides in the Ascidian-Marine drugs · 2022Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Recent advances in the biosynthesis of RiPPs from multicore-containing precursor peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Expanding the chemical space of synthetic cyclic peptides using a promiscuous macrocyclase from prenylagaramide biosynthesis.ACS catalysis · 2020Article
- Roads to Rome: Role of Multiple Cassettes in Cyanobactin RiPP Biosynthesis.Journal of the American Chemical Society · 2018Article
- Biosynthetic Proteases That Catalyze the Macrocyclization of Ribosomally Synthesized Linear Peptides.Biochemistry · 2018Review
- Parallel lives of symbionts and hosts: chemical mutualism in marine animals.Natural product reports · 2018Review
- The Biochemistry and Structural Biology of Cyanobactin Pathways: Enabling Combinatorial Biosynthesis.Methods in enzymology · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Biocatalysis is a fast developing field in which an enzyme's natural capabilities are harnessed or engineered for synthetic chemistry. The enzyme PatG is an extremely promiscuous macrocyclase enzyme tolerating both non-natural amino acids and non-amino acids within the substrate. It does, however, require a proline or thiazoline at the C-terminal position of the core peptide which means the final product must contain this group. Here, we show guided by structural insight we have identified two synthetic routes, triazole and a double cysteine, that circumvent this requirement. With the triazole, we show PatGmac can macrocyclise substrates that do not contain any amino acids in the final product.
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Registered trials
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