ReviewACS bio & med chem Au2024
Bacterial Cytochrome P450 Catalyzed Macrocyclization of Ribosomal Peptides.
Review in ACS bio & med chem Au, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- P450 cyptide synthase KwwB catalyzes non-native cross-link at Tyr-C3-Trp-N1 and tolerates leader peptide mutations.The Journal of antibiotics · 2026Article
- Reprogramming RiPP scaffolds through skeletal editing unlocks chemical space.Chemical science · 2026Article
- Unified Access to Biaryl-Bridged Linkages Unlocks Structural Diversification of Noncanonical Cyclic Peptides.Journal of the American Chemical Society · 2026Article
- P450 Cyptide Synthase AscB Catalyzes Fused Cyclophane at the YxWxH Motif on the Precursor Peptides.Organic letters · 2026Article
- P450 Cyptide Synthase KwwB Catalyzes Trp-C5-Trp-N1 Cross-Linking and Accepts Diverse Precursor Peptides.Organic letters · 2026Article
- Biosynthesis of Biphenomycin-like Macrocyclic Peptides by Formation and Cross-Linking ofJournal of the American Chemical Society · 2025Article
- The Deep Mining Era: Genomic, Metabolomic, and Integrative Approaches to Microbial Natural Products from 2018 to 2024.Marine drugs · 2025Review
- P450 Biarylitide Synthase ShyB Catalyzes the Cross-Link Between His-C2 and Tyr-O4 on the Precursor Peptide.Organic letters · 2025Article
- Biosynthesis of Macrocyclic Peptides by Formation and Crosslinking ofbioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Macrocyclization is a vital process in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), significantly enhancing their structural diversity and biological activity. Universally found in living organisms, cytochrome P450 enzymes (P450s) are versatile catalysts that facilitate a wide array of chemical transformations and have recently been discovered to contribute to the expansion and complexity of the chemical spectrum of RiPPs. Particularly, P450-catalyzed biaryl-bridged RiPPs, characterized by highly modified structures, represent an intriguing but underexplored class of natural products, as demonstrated by the recent discovery of tryptorubin A, biarylitide and cittilin. These P450 enzymes demonstrate their versatility by facilitating peptide macrocyclization through the formation of carbon-carbon (C-C), carbon-nitrogen (C-N) and ether bonds between the side chains of tyrosine (Tyr), tryptophan (Trp) and histidine (His). This Review briefly highlights the latest progress in P450-catalyzed macrocyclization within RiPP biosynthesis, resulting in the generation of structurally complex RiPPs. These findings have expedited the discovery and detailed analysis of new P450s engaged in RiPP biosynthetic pathways.
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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.