Exploring RiPP-derived N -acyltransferases for genetically encoded lipopeptide engineering
Year: 2026
Type: article
Abstract: -acyltransferases as biocatalysts, we probed the peptide substrate specificity of the model lauroyl-transferase KspN from kamptornamide biosynthesis. Nearest-neighbor, lysine-scan, and truncation mutants demonstrated promiscuity for the peptide substrate. As a proof-of-concept toward designer lipopeptides using RiPP biosynthetic principles, we produced sequences mimicking bioactive non-ribosomal lipopeptides and tested their conversion by maturases from the kamptornamide biosynthetic pathway. Ornithines, fatty acyl groups, and lanthionine macrocycles were installed in the mimics as a promising start toward the directed biosynthesis of custom lipopeptides.
Source: RSC Chemical Biology
DOI: 10.1039/d6cb00169f
Institutions: ETH Zurich, Institute of Microbiology
Language: English
Subfield: Applied Microbiology and Biotechnology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,962
OpenAlex ID: W7220660428