ArticleACS chemical biology2018
Characterization of the Fast and Promiscuous Macrocyclase from Plant PCY1 Enables the Use of Simple Substrates.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Discovery and development of penicillin-binding protein-type thioesterases as biocatalysts.Current opinion in biotechnology · 2026Review
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Assessing Substrate Scope of the Cyclodehydratase LynD by mRNA Display-Enabled Machine Learning Models.Biochemistry · 2025Article
- Identification of a key peptide cyclase for novel cyclic peptide discovery in Pseudostellaria heterophylla.Plant communications · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Plant peptides - redefining an area of ribosomally synthesized and post-translationally modified peptides.Natural product reports · 2024Review
- 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
- Biocatalytic cyclization of small macrolactams by a penicillin-binding protein-type thioesterase.Nature chemical biology · 2024Article
- Biochemical characterization of a cyanobactin arginine-Chemical communications (Cambridge, England) · 2022Article
- Applying Promiscuous RiPP Enzymes to Peptide BackboneACS chemical biology · 2022Article
- Accessing Diverse Pyridine-Based Macrocyclic Peptides by a Two-Site Recognition Pathway.Journal of the American Chemical Society · 2022Article
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- Macrocylases as synthetic tools for ligand synthesis: enzymatic synthesis of cyclic peptides containing metal-binding amino acids.Royal Society open science · 2021Article
- Enzymatic Synthesis Assisted Discovery of Proline-Rich Macrocyclic Peptides in Marine Sponges.Chembiochem : a European journal of chemical biology · 2021Article
- Asparaginyl endopeptidases: enzymology, applications and limitations.Organic & biomolecular chemistry · 2021Review
- 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
- Recent Advances in the Discovery and Biosynthetic Study of Eukaryotic RiPP Natural Products.Molecules (Basel, Switzerland) · 2019Review
- Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.ACS chemical biology · 2018Article
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cyclic ribosomally derived peptides possess diverse bioactivities and are currently of major interest in drug development. However, it can be chemically challenging to synthesize these molecules, hindering the diversification and testing of cyclic peptide leads. Enzymes used in vitro offer a solution to this; however peptide macrocyclization remains the bottleneck. PCY1, involved in the biosynthesis of plant orbitides, belongs to the class of prolyl oligopeptidases and natively displays substrate promiscuity. PCY1 is a promising candidate for in vitro utilization, but its substrates require an 11 to 16 residue C-terminal recognition tail. We have characterized PCY1 both kinetically and structurally with multiple substrate complexes revealing the molecular basis of recognition and catalysis. Using these insights, we have identified a three residue C-terminal extension that replaces the natural recognition tail permitting PCY1 to operate on synthetic substrates. We demonstrate that PCY1 can macrocyclize a variety of substrates with this short tail, including unnatural amino acids and nonamino acids, highlighting PCY1's potential in biocatalysis.
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