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

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

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Title: Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring
Author: Zha, Li; Jiang, Yindi; Henke, Matthew T.; Wilson, Matthew R.; Wang, Jennifer X.; Kelleher, Neil L.; Balskus, Emily P.

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Citation: 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.
Published Version: doi:10.1038/nchembio.2448
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5657534/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:35015083
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