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- W2777114057 abstract "Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing family of bioactive peptides. Among RiPPs, the bacterial toxin polytheonamide A is characterized by a unique set of post-translational modifications catalyzed by novel radical S-adenosyl-l-methionine (SAM) enzymes. Here we show that the radical SAM enzyme PoyD catalyzes in vitro polytheonamide epimerization in a C-to-N directional manner. By combining mutagenesis experiments with labeling studies and investigating the enzyme substrate promiscuity, we deciphered in detail the mechanism of PoyD. We notably identified a critical cysteine residue as a likely key H atom donor and demonstrated that PoyD belongs to a distinct family of radical SAM peptidyl epimerases. In addition, our study shows that the core peptide directly influences the epimerization pattern allowing for production of peptides with unnatural epimerization patterns." @default.
- W2777114057 created "2018-01-05" @default.
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- W2777114057 date "2018-02-06" @default.
- W2777114057 modified "2023-10-12" @default.
- W2777114057 title "Mechanistic Investigations of PoyD, a Radical <i>S</i>-Adenosyl-<scp>l</scp>-methionine Enzyme Catalyzing Iterative and Directional Epimerizations in Polytheonamide A Biosynthesis" @default.
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- W2777114057 doi "https://doi.org/10.1021/jacs.7b08402" @default.
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