@article{429802865f9f47e782f326e49f8f9503,
title = "Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring",
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.",
author = "Li Zha and Yindi Jiang and Henke, {Matthew T.} and Wilson, {Matthew R.} and Wang, {Jennifer X.} and Kelleher, {Neil L.} and Balskus, {Emily P.}",
note = "Funding Information: We thank C. Brotherton and A. Sieg for help with cloning; J. May (Kahne lab, Harvard University, Cambridge, MA) for help with radiometric assays; M. McCallum for help with bioinformatic analyses; and P. Boudreau, C. Chittim, D. Kenny, H. Nakamura, and S. Peck for helpful discussions. L.Z., Y.J., M.R.W., and E.P.B. acknowledge financial support from National Cancer Institute (1R01CA208834-01), the Damon Runyon–Rachleff Innovation Award, and the Packard Fellowship for Science and Engineering. M.T.H. and N.L.K. were supported by Northwestern University and the US National Institutes of Health (GM 067725 and AT 009143). M.R.W. is supported by an American Cancer Society-New England Division Postdoctoral Fellowship (PF-16-122-01-CDD). Publisher Copyright: {\textcopyright} 2017 Nature America, Inc., part of Springer Nature. All rights reserved.",
year = "2017",
month = oct,
day = "1",
doi = "10.1038/nchembio.2448",
language = "English (US)",
volume = "13",
pages = "1063--1065",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "10",
}