| Literature DB >> 32109054 |
Steven R Fleming1, Paul M Himes1, Swapnil V Ghodge1,2, Yuki Goto3,4, Hiroaki Suga3,5, Albert A Bowers1.
Abstract
PaaA is a RiPP enzyme that catalyzes the transformation of two glutamic acid residues within a substrate peptide into the bicyclic core of Pantocin A. Here, for the first time, we use mRNA display techniques to understand RiPP enzyme-substrate interactions to illuminate PaaA substrate recognition. Additionally, our data revealed insights into the enzymatic timing of glutamic acid modification. The technique developed is quite sensitive and a significant advancement over current RiPP studies and opens the door to enzyme modified mRNA display libraries for natural product-like inhibitor pans.Entities:
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Year: 2020 PMID： 32109054 PMCID： PMC7330867 DOI： 10.1021/jacs.0c01576
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419