ArticleJournal of the American Chemical Society2019
Enzymatic Reconstitution and Biosynthetic Investigation of the Lasso Peptide Fusilassin.
Article in Journal of the American Chemical Society, 2019. 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, 98 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Peptide-Based Pseudo[2]- and [3]rotaxanes Assembled via Square-Planar Palladium Coordination.ChemPlusChem · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.Analytical chemistry · 2025Article
- Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025Article
- LassoESM a tailored language model for enhanced lasso peptide property prediction.Nature communications · 2025Article
- Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025Review
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- LassoPred: a tool to predict the 3D structure of lasso peptides.Nature communications · 2025Article
- In silico design of foldable lasso peptides.Biophysical journal · 2025Article
- Substrate interactions guide cyclase engineering and lasso peptide diversification.Nature chemical biology · 2025Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- Advances in lasso peptide discovery, biosynthesis, and function.Trends in genetics : TIG · 2024Review
- Structure Prediction and Protein Engineering Yield New Insights into Microcin J25 Precursor Recognition.ACS chemical biology · 2024Article
- Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides.Journal of the American Chemical Society · 2024Article
- One Descriptor to Fold Them All: Harnessing Intuition and Machine Learning to Identify Transferable Lasso Peptide Reaction Coordinates.The journal of physical chemistry. B · 2024Article
- Article
- Lasso Peptides: Exploring the Folding Landscape of Nature's Smallest Interlocked Motifs.Journal of the American Chemical Society · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Lasso peptides are a class of ribosomally synthesized and post-translationally modified natural product which possess a unique lariat knot conformation. The low entropy "threaded" conformation endows lasso peptides with considerable resistance to heat and proteolytic degradation, which are attractive properties for the development of peptide-based therapeutics. Despite their discovery nearly 30 years ago, the molecular mechanism underlying lasso peptide biosynthesis remains poorly characterized due to the low stability of the purified biosynthetic enzymes. Here, we report the biosynthetic reconstitution of a lasso peptide derived from Thermobifida fusca, termed fusilassin. Beyond robust catalytic activity, the fusilassin enzymes demonstrate extraordinary substrate tolerance during heterologous expression in E. coli and upon purification in cell-free biosynthetic reconstitution reactions. We provide evidence that the fusilassin biosynthetic enzymes are not capable of forming branched-cyclic products but can produce entirely unrelated lasso peptides. Finally, we leveraged our bioinformatic survey of all lasso peptides identified in GenBank to perform coevolutionary analysis of two requisite biosynthetic proteins. This effort correctly identified residues governing an important protein-protein interaction, illustrating how genomic insight can accelerate the characterization of natural product biosynthetic pathways. The fusilassin enzymes described within represent a model system for both designing future lasso peptides of biomedical importance and also for elucidating the molecular mechanisms that govern lasso peptide biosynthesis.
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Registered trials
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.