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Wilson, Matthew

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Wilson

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Matthew

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Wilson, Matthew

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Author's Publications: search.filters.isAuthorOfPublication.30e1490e-419d-4e26-9812-be6aa3bfc724

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    Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring
    (2017) Zha, Li; Jiang, Yindi; Henke, Matthew T.; Wilson, Matthew; Wang, Jennifer X.; Kelleher, Neil L.; Balskus, Emily
    Despite containing an α-amino acid, the versatile cofactor S-adenosylmethionine (SAM) is not a known building block for non-ribosomal peptide synthetase (NRPS) assembly lines. Here we report an unusual NRPS module from colibactin biosynthesis that uses SAM for amide bond formation and subsequent cyclopropanation. Our findings showcase a new use for SAM and reveal a novel biosynthetic route to a functional group that likely mediates colibactin’s genotoxicity.
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    Production of Stealthin C Involves an S–N-Type Smiles Rearrangement
    (American Chemical Society (ACS), 2017) Wang, Peng; Hong, Gloria J.; Wilson, Matthew; Balskus, Emily
    The kinamycin family of aromatic polyketide natural products contains an atypical angucycline ring system substituted with a diazo group. The enzymatic chemistry involved in constructing both of these structural features has been largely unexplored. Here we report the in vivo and in vitro production of seongomycin, a shunt product from this pathway, and stealthin C, a proposed biosynthetic precursor to the kinamycins. We show that a single enzyme, the flavin-dependent monooxygenase AlpJ, can generate these metabolites from N-acetyl-l-cysteine and l-cysteine, respectively, and that the synthesis of stealthin C likely proceeds via a nonenzymatic S–N-type Smiles rearrangement. This unexpected route to stealthin C reveals a distinct approach to install aromatic amino groups in metabolites and raises questions about the intermediacy of this species in kinamycin production.