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• W2092773485 abstract "Syringolins are a class of cyclic tripeptide natural products that are potent and irreversible inhibitors of the eukaryotic proteasome. In addition to being hybrid NRPS/PKS molecules, they also feature an unusual ureido-linkage (red) between two amino acid monomers. Here we report the first in vitro characterization of enzymatic ureido-linkage formation which is catalyzed by an NRPS, SylC. Using (13)C- and (18)O-labeling studies, we show that biosynthesis occurs via N-carboxylation to form an initial N-carboxy-aminoacyl-S-Ppant enzyme intermediate which undergoes intramolecular cyclization followed by condensation with a second amino acid to form the ureido-containing dipeptide product." @default.
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• W2092773485 date "2009-12-07" @default.
• W2092773485 modified "2023-10-01" @default.
• W2092773485 title "SylC Catalyzes Ureido-Bond Formation During Biosynthesis of the Proteasome Inhibitor Syringolin A" @default.
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• W2092773485 doi "https://doi.org/10.1021/ja909170u" @default.
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