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

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.

SUBMITTER: Baulig A

PROVIDER: S-EPMC6482885 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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

Baulig Alexandra A Helmle Irina I Bader Marius M Wolf Felix F Kulik Andreas A Al-Dilaimi Arwa A Wibberg Daniel D Kalinowski Jörn J Gross Harald H Kaysser Leonard L

Chemical science 20190321 16

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 <i>via</i> a phosphoramidate bridge. Herein, we report the identification of a gene cluster for the formation of phosphoramidon and its detailed characterization. <i>In vitro</i> reconstitution of the biosynthesis established TalE as a phosphoramidate-forming kinase and TalC as the glycosyltransferase which installs the l- ...[more]

PMID: 31057776

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