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


ABSTRACT: Despite containing an ?-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.

SUBMITTER: Zha L 

PROVIDER: S-EPMC5657534 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

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

Zha Li L   Jiang Yindi Y   Henke Matthew T MT   Wilson Matthew R MR   Wang Jennifer X JX   Kelleher Neil L NL   Balskus Emily P EP  

Nature chemical biology 20170807 10


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. ...[more]

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