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

doi:10.1038/nchembio.2448

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

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

43 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 language	English (US)
Pages (from-to)	1063-1065
Number of pages	3
Journal	Nature Chemical Biology
Volume	13
Issue number	10
DOIs	https://doi.org/10.1038/nchembio.2448
State	Published - Oct 1 2017

ASJC Scopus subject areas

Molecular Biology
Cell Biology

Access to Document

10.1038/nchembio.2448

Cite this

@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.}",

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 Research",

number = "10",

}

TY - JOUR

T1 - Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring

AU - Zha, Li

AU - Jiang, Yindi

AU - Henke, Matthew T.

AU - Wilson, Matthew R.

AU - Wang, Jennifer X.

AU - Kelleher, Neil L.

AU - Balskus, Emily P.

PY - 2017/10/1

Y1 - 2017/10/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85031099481&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85031099481&partnerID=8YFLogxK

U2 - 10.1038/nchembio.2448

DO - 10.1038/nchembio.2448

M3 - Article

C2 - 28805802

AN - SCOPUS:85031099481

SN - 1552-4450

VL - 13

SP - 1063

EP - 1065

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 10

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this