ArticleACS central science2022
Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates.
Article in ACS central science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026Article
- Leaderless RiPPs expand the repertoire of fungal secondary metabolites.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- A peptide dehydratase with core strength.Nature chemical biology · 2024Article
- Genome Mining for New Enzyme Chemistry.ACS catalysis · 2024Review
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Discovery, Function, and Engineering of Graspetides.Trends in chemistry · 2023Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Cell-free Biosynthesis of Peptidomimetics.Biotechnology and bioprocess engineering : BBE · 2023Review
- Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM.ACS synthetic biology · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Bioinformatic prediction and experimental validation of RiPP recognition elements.Methods in enzymology · 2023Article
- Article
- Control of Nucleophile Chemoselectivity in Cyanobactin YcaO Heterocyclases PatD and TruD.ACS chemical biology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are peptide-derived natural products with potent antibiotic, antiviral, and anticancer properties. RiPP enzymes known as cyclodehydratases and dehydrogenases work together to catalyze intramolecular, inter-residue condensation and dehydrogenation reactions that install oxazoline/oxazole and thiazoline/thiazole heterocycles within ribosomally produced polypeptide chains. Here, we show that the previously reported enzymes MicD-F and ArtGox accept backbone-modified monomers-including aminobenzoic acid derivatives and beta-amino acids-within leader-free polypeptides, even at positions immediately preceding or following the site of cyclization/dehydrogenation. The products are sequence-defined chemical polymers with multiple, diverse non-α-amino acid subunits. We show further that MicD-F and ArtGox can install heterocyclic backbones within protein loops and linkers without disrupting the native tertiary fold. Calculations reveal the extent to which these heterocycles restrict conformational space; they also eliminate a peptide bond-both features could improve the stability or add function to linker sequences now commonplace in emerging biotherapeutics. This work represents a general strategy to expand the chemical diversity of the proteome beyond and in synergy with what can now be accomplished by expanding the genetic code.
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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.