ArticleProceedings of the National Academy of Sciences of the United States of America2017
Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 70 citations in OpenAlex.
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- Biosynthesis of 14-membered cyclopeptide alkaloids via non-heme-iron- and 2-oxoglutarate-dependent oxidative decarboxylation.bioRxiv : the preprint server for biology · 2026Article
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Identification of a key peptide cyclase for novel cyclic peptide discovery in Pseudostellaria heterophylla.Plant communications · 2025Article
- α/β Hydrolases: Toward Unraveling Entangled Classification.Proteins · 2025Article
- Anticancer Ribosomally Synthesized and Post-Translationally Modified Peptides from Plants: Structures, Therapeutic Potential, and Future Directions.Current issues in molecular biology · 2024Review
- Plant peptides - redefining an area of ribosomally synthesized and post-translationally modified peptides.Natural product reports · 2024Review
- Biosynthesis of Strained Amino Acids Through a PLP-Dependent Enzyme via Cryptic Halogenation.bioRxiv : the preprint server for biology · 2023Article
- AlphaFold Accurately Predicts the Structure of Ribosomally Synthesized and Post-Translationally Modified Peptide Biosynthetic Enzymes.Biomolecules · 2023Article
- Native and Engineered Cyclic Disulfide-Rich Peptides as Drug Leads.Molecules (Basel, Switzerland) · 2023Review
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Applying Promiscuous RiPP Enzymes to Peptide BackboneACS chemical biology · 2022Article
- The flax genome reveals orbitide diversity.BMC genomics · 2022Article
- Discovery and biosynthesis of cyclic plant peptides via autocatalytic cyclases.Nature chemical biology · 2022Article
- Vypal2: A Versatile Peptide Ligase for Precision Tailoring of Proteins.International journal of molecular sciences · 2021Article
- Macrocylases as synthetic tools for ligand synthesis: enzymatic synthesis of cyclic peptides containing metal-binding amino acids.Royal Society open science · 2021Article
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- Review
- Plant asparaginyl endopeptidases and their structural determinants of function.Biochemical Society transactions · 2021Review
- Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site.Journal of the American Chemical Society · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Enzymes that can catalyze the macrocyclization of linear peptide substrates have long been sought for the production of libraries of structurally diverse scaffolds via combinatorial gene assembly as well as to afford rapid in vivo screening methods. Orbitides are plant ribosomally synthesized and posttranslationally modified peptides (RiPPs) of various sizes and topologies, several of which are shown to be biologically active. The diversity in size and sequence of orbitides suggests that the corresponding macrocyclases may be ideal catalysts for production of cyclic peptides. Here we present the biochemical characterization and crystal structures of the plant enzyme PCY1 involved in orbitide macrocyclization. These studies demonstrate how the PCY1 S9A protease fold has been adapted for transamidation, rather than hydrolysis, of acyl-enzyme intermediates to yield cyclic products. Notably, PCY1 uses an unusual strategy in which the cleaved C-terminal follower peptide from the substrate stabilizes the enzyme in a productive conformation to facilitate macrocyclization of the N-terminal fragment. The broad substrate tolerance of PCY1 can be exploited as a biotechnological tool to generate structurally diverse arrays of macrocycles, including those with nonproteinogenic elements.
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