ArticleACS central science2019
Mechanistic Basis for Ribosomal Peptide Backbone Modifications.
Article in ACS central science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Backbone Thioamidation of a Ribosomal Subunit Protein in Pseudomonadota.Biochemistry · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- Biosynthesis of peptide-nucleobase hybrids in ribosomal peptides.Nature chemical biology · 2025Article
- Darobactin Substrate Engineering and Computation Show Radical Stability Governs Ether versus C-C Bond Formation.Journal of the American Chemical Society · 2024Article
- General Installation of (4Journal of the American Chemical Society · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- Thioimidates provide general access to thioamide, amidine, and imidazolone peptide-bond isosteres.Methods in enzymology · 2024Article
- Benzylic Radical Stabilization Permits Ether Formation During Darobactin Biosynthesis.bioRxiv : the preprint server for biology · 2023Article
- AlphaFold Accurately Predicts the Structure of Ribosomally Synthesized and Post-Translationally Modified Peptide Biosynthetic Enzymes.Biomolecules · 2023Article
- Article
- Bioconjugate Platform for Iterative BackboneACS catalysis · 2022Article
- Site-Selective Amide Functionalization by Catalytic Azoline Engrafting.ACS catalysis · 2022Article
- Accurate Models of Substrate Preferences of Post-Translational Modification Enzymes from a Combination of mRNA Display and Deep Learning.ACS central science · 2022Article
- Control of Nucleophile Chemoselectivity in Cyanobactin YcaO Heterocyclases PatD and TruD.ACS chemical biology · 2022Article
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- Discovery and characterisation of an amidine-containing ribosomally-synthesised peptide that is widely distributed in nature.Chemical science · 2021Article
- Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis.Nature communications · 2021Article
- Functional elucidation of TfuA in peptide backbone thioamidation.Nature chemical biology · 2021Article
- Understanding thioamitide biosynthesis using pathway engineering and untargeted metabolomics.Chemical science · 2021Article
- Global Genome Mining Reveals the Distribution of Diverse Thioamidated RiPP Biosynthesis Gene Clusters.Frontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
YcaO enzymes are known to catalyze the ATP-dependent formation of azoline heterocycles, thioamides, and (macro)lactamidines on peptide substrates. These enzymes are found in multiple biosynthetic pathways, including those for several different classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). However, there are major knowledge gaps in the mechanistic and structural underpinnings that govern each of the known YcaO-mediated modifications. Here, we present the first structure of any YcaO enzyme bound to its peptide substrate in the active site, specifically that from
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