Publication: Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring
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2017
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Zha, Li, Yindi Jiang, Matthew T. Henke, Matthew R. Wilson, Jennifer X. Wang, Neil L. Kelleher, and Emily P. Balskus. 2017. “Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring.” Nature chemical biology 13 (10): 1063-1065. doi:10.1038/nchembio.2448. http://dx.doi.org/10.1038/nchembio.2448.
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Abstract
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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