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Chem Sci. 2019 Mar 21;10(16):4486-4490. doi: 10.1039/c9sc00641a. eCollection 2019 Apr 28.

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

Author information

1
Department of Pharmaceutical Biology , Pharmaceutical Institute , University of Tübingen , 72076 Tübingen , Germany . Email: leonard.kaysser@uni-tuebingen.de.
2
German Centre for Infection Research (DZIF) , partner site Tübingen , 72076 Tübingen , Germany.
3
Interfaculty Institute for Microbiology and Infection Medicine Tübingen (IMIT) , Microbiology/Biotechnology , University of Tübingen , 72076 Tübingen , Germany.
4
Center for Biotechnology (CeBiTec) , Bielefeld University , 33615 Bielefeld , Germany.

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.

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