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The biarylitides: understanding the structure and biosynthesis of a fascinating class of Cytochrome P450 modified RiPP natural products. | LitMetric

The biarylitides: understanding the structure and biosynthesis of a fascinating class of Cytochrome P450 modified RiPP natural products.

Chembiochem

Monash University, Department of Biochemistry and Molecular Biology, 15 Innovation Walk, Monash University, 3800, Melbourne, AUSTRALIA.

Published: December 2024

AI Article Synopsis

  • The biarylitides are a newly identified group of natural products known for their small core peptides and varied peptide crosslinking facilitated by cytochrome P450 enzymes.
  • This review focuses on the discovery and biosynthetic diversity of biarylitides, highlighting both the methods and challenges in analyzing their cyclic peptide structures.
  • It also explores the structures of the P450 enzymes connected to these biarylitides and examines their potential alternate catalytic functions as demonstrated in rufomycin biosynthesis.

Article Abstract

The biarylitides are a recently discovered class of RiPP natural products that are fascinating both from the small size of the core peptides as well as the diversity of peptide crosslinking exhibited by the cytochrome P450 enzymes found in these systems. In this review, we address the discovery and biosynthetic diversity of these systems and discuss the methods and challenges of analysing the structures of these constrained cyclic peptides. We also discuss the structures of the P450 enzymes involved in these pathways and address the potential for alternate catalytic outcomes and activities as seen most recently with the inclusion of biarylitide related enzymes within rufomycin biosynthesis.

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Source
http://dx.doi.org/10.1002/cbic.202400916DOI Listing

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