A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli

Ann E. Donnelly; Grant S. Murphy; Katherine M. Digianantonio; Michael H. Hecht

doi:10.1038/nchembio.2550

A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli

Ann E. Donnelly
, Grant S. Murphy
, Katherine M. Digianantonio
, Michael H. Hecht

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

47 Scopus citations

Abstract

Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that meets both criteria. Purified Syn-F4 hydrolyzes the siderophore ferric enterobactin, and expression of Syn-F4 allows an inviable strain of Escherichia coli to grow in iron-limited medium. These findings demonstrate that entirely new sequences can provide life-sustaining enzymatic functions in living organisms.

Original language	English (US)
Pages (from-to)	253-255
Number of pages	3
Journal	Nature Chemical Biology
Volume	14
Issue number	3
DOIs	https://doi.org/10.1038/nchembio.2550
State	Published - Mar 1 2018

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1038/nchembio.2550

Cite this

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title = "A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli",

abstract = "Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that meets both criteria. Purified Syn-F4 hydrolyzes the siderophore ferric enterobactin, and expression of Syn-F4 allows an inviable strain of Escherichia coli to grow in iron-limited medium. These findings demonstrate that entirely new sequences can provide life-sustaining enzymatic functions in living organisms.",

author = "Donnelly, \{Ann E.\} and Murphy, \{Grant S.\} and Digianantonio, \{Katherine M.\} and Hecht, \{Michael H.\}",

note = "Funding Information: We thank J. Eng for assistance with LC–MS and E. Nolan (MIT) for providing D-enterobactin. This work was funded by NSF Grant MCB-1409402, and by the Department of Defense (DoD) through the National Defense Science \& Engineering Graduate Fellowship (NDSEG) Program to A.E.D. Funding Information: We thank J. Eng for assistance with LCMS and E. Nolan (MIT) for providing D-enterobactin. This work was funded by NSF Grant MCB-1409402, and by the Department of Defense (DoD) through the National Defense Science \& Engineering Graduate Fellowship (NDSEG) Program to A.E.D.",

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doi = "10.1038/nchembio.2550",

language = "English (US)",

volume = "14",

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journal = "Nature Chemical Biology",

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AU - Donnelly, Ann E.

AU - Murphy, Grant S.

AU - Digianantonio, Katherine M.

AU - Hecht, Michael H.

N1 - Funding Information: We thank J. Eng for assistance with LC–MS and E. Nolan (MIT) for providing D-enterobactin. This work was funded by NSF Grant MCB-1409402, and by the Department of Defense (DoD) through the National Defense Science & Engineering Graduate Fellowship (NDSEG) Program to A.E.D. Funding Information: We thank J. Eng for assistance with LCMS and E. Nolan (MIT) for providing D-enterobactin. This work was funded by NSF Grant MCB-1409402, and by the Department of Defense (DoD) through the National Defense Science & Engineering Graduate Fellowship (NDSEG) Program to A.E.D.

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AB - Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Here we describe Syn-F4, the first de novo protein that meets both criteria. Purified Syn-F4 hydrolyzes the siderophore ferric enterobactin, and expression of Syn-F4 allows an inviable strain of Escherichia coli to grow in iron-limited medium. These findings demonstrate that entirely new sequences can provide life-sustaining enzymatic functions in living organisms.

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DO - 10.1038/nchembio.2550

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ER -

A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli

Abstract

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