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Issue 16, 2019
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Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N–P-bond-forming kinase

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Abstract

Phosphoramidon is a potent metalloprotease inhibitor and a widespread tool in cell biology research. It contains a dipeptide backbone that is uniquely linked to a 6-deoxysugar via a phosphoramidate bridge. Herein, we report the identification of a gene cluster for the formation of phosphoramidon and its detailed characterization. In vitro reconstitution of the biosynthesis established TalE as a phosphoramidate-forming kinase and TalC as the glycosyltransferase which installs the L-rhamnose moiety by phosphoester linkage.

Graphical abstract: Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N–P-bond-forming kinase

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Publication details

The article was received on 05 Feb 2019, accepted on 11 Mar 2019 and first published on 21 Mar 2019


Article type: Edge Article
DOI: 10.1039/C9SC00641A
Chem. Sci., 2019,10, 4486-4490
  • Open access: Creative Commons BY-NC license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N–P-bond-forming kinase

    A. Baulig, I. Helmle, M. Bader, F. Wolf, A. Kulik, A. Al-Dilaimi, D. Wibberg, J. Kalinowski, H. Gross and L. Kaysser, Chem. Sci., 2019, 10, 4486
    DOI: 10.1039/C9SC00641A

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