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

Li Zha, Yindi Jiang, Matthew T. Henke, Matthew R. Wilson, Jennifer X. Wang, Neil L. Kelleher*, Emily P. Balskus

*Corresponding author for this work

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1063-1065
Number of pages3
JournalNature Chemical Biology
Volume13
Issue number10
DOIs
StatePublished - Oct 1 2017

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Zha, L., Jiang, Y., Henke, M. T., Wilson, M. R., Wang, J. X., Kelleher, N. L., & Balskus, E. P. (2017). Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring. Nature Chemical Biology, 13(10), 1063-1065. https://doi.org/10.1038/nchembio.2448