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• W3047654533 endingPage "2054" @default.
• W3047654533 startingPage "2048" @default.
• W3047654533 abstract "Lincosamides are clinically important antibiotics originally produced as microbial specialized metabolites. The complex biosynthesis of lincosamides is coupled to the metabolism of mycothiol as a sulfur donor. Here, we elucidated the N-deacetylation of the mycothiol-derived N-acetyl-l-cysteine residue of a lincosamide intermediate, which is comprised of an amino acid and an aminooctose connected via an amide bond. We purified this intermediate from the culture broth of a deletion mutant strain and tested it as a substrate of recombinant lincosamide biosynthetic proteins in the in vitro assays that were monitored via liquid chromatography–mass spectrometry. Our findings showed that the N-deacetylation reaction is catalyzed by CcbIH/CcbQ or LmbIH/LmbQ proteins in celesticetin and lincomycin biosynthesis, respectively. These are the first N-deacetylases from the TldD/PmbA protein family, from which otherwise only several proteases and peptidases were functionally characterized. Furthermore, we present a sequence similarity network of TldD/PmbA proteins, which suggests that the lincosamide N-deacetylases are unique among these widely distributed proteins." @default.
• W3047654533 created "2020-08-13" @default.
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• W3047654533 date "2020-08-06" @default.
• W3047654533 modified "2023-09-30" @default.
• W3047654533 title "<i>N</i>-Deacetylation in Lincosamide Biosynthesis Is Catalyzed by a TldD/PmbA Family Protein" @default.
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• W3047654533 doi "https://doi.org/10.1021/acschembio.0c00224" @default.
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