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The B12-Radical SAM Enzyme PoyC Catalyzes Valine Cβ‑Methylation during Polytheonamide Biosynthesis

Parent, Aubérie ; Guillot, Alain ; Benjdia, Alhosna ; Chartier, Gwladys ; Leprince, Jérôme ; Berteau, Olivier

Journal of the American Chemical Society, 2016-12, Vol.138 (48), p.15515-15518 [Periódico revisado por pares]

American Chemical Society

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  • Título:
    The B12-Radical SAM Enzyme PoyC Catalyzes Valine Cβ‑Methylation during Polytheonamide Biosynthesis
  • Autor: Parent, Aubérie ; Guillot, Alain ; Benjdia, Alhosna ; Chartier, Gwladys ; Leprince, Jérôme ; Berteau, Olivier
  • Assuntos: Communication
  • É parte de: Journal of the American Chemical Society, 2016-12, Vol.138 (48), p.15515-15518
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: Genomic and metagenomic investigations have recently led to the delineation of a novel class of natural products called ribosomally synthesized and post-translationally modified peptides (RiPPs). RiPPs are ubiquitous among living organisms and include pharmaceutically relevant compounds such as antibiotics and toxins. A prominent example is polytheonamide A, which exhibits numerous post-translational modifications, some of which were unknown in ribosomal peptides until recently. Among these post-translational modifications, C-methylations have been proposed to be catalyzed by two putative radical S-adenosylmethionine (rSAM) enzymes, PoyB and PoyC. Here we report the in vitro activity of PoyC, the first B12-dependent rSAM enzyme catalyzing peptide Cβ-methylation. We show that PoyC catalyzes the formation of S-adenosylhomocysteine and 5′-deoxyadenosine and the transfer of a methyl group to l-valine residue. In addition, we demonstrate for the first time that B12-rSAM enzymes have a tightly bound MeCbl cofactor that during catalysis transfers a methyl group originating from S-adenosyl-l-methionine. Collectively, our results shed new light on polytheonamide biosynthesis and the large and emerging family of B12-rSAM enzymes.
  • Editor: American Chemical Society
  • Idioma: Inglês
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