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• W3100492067 endingPage "20334" @default.
• W3100492067 startingPage "20329" @default.
• W3100492067 abstract "We report a method for the high-throughput reactivity profiling of genetically encoded libraries as a tool to study substrate fitness landscapes for RiPP (ribosomally synthesized and post-translationally modified peptide) biosynthetic enzymes. This method allowed us to rapidly analyze the substrate preferences of the lactazole biosynthetic pathway using a saturation mutagenesis mRNA display library of lactazole precursor peptides. We demonstrate that the assay produces accurate and reproducible in vitro data, enabling the quantification of reaction yields with temporal resolution. Our results recapitulate the previously established knowledge on lactazole biosynthesis and expand it by identifying the extent of substrate promiscuity exhibited by the enzymes. This work lays a foundation for the construction and screening of mRNA display-based combinatorial thiopeptide libraries for the discovery of lactazole-inspired thiopeptides with de novo designed biological activities." @default.
• W3100492067 created "2020-11-23" @default.
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• W3100492067 date "2020-11-19" @default.
• W3100492067 modified "2023-10-16" @default.
• W3100492067 title "Accurate Broadcasting of Substrate Fitness for Lactazole Biosynthetic Pathway from Reactivity-Profiling mRNA Display" @default.
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• W3100492067 doi "https://doi.org/10.1021/jacs.0c10374" @default.
• W3100492067 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33211968" @default.
• W3100492067 hasPublicationYear "2020" @default.
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