Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring
Nature chemical biology, 2017•nature.com
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.
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.
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.
nature.com
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