Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring

August 7th, 2017 by Li Zha

Nature Chemical Biology 13, 1063 (2017). doi:10.1038/nchembio.2448

Authors: Li Zha, Yindi Jiang, Matthew T Henke, Matthew R Wilson, Jennifer X Wang, Neil L Kelleher & Emily P Balskus

Despite containing an α-amino acid, the versatile cofactor S-adenosylmethionine (SAM) is not a known building block for nonribosomal 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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