Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N–P-bond-forming kinase. Issue 16 (21st March 2019)

• Record Type: Journal Article
• Authors: Baulig, Alexandra; Helmle, Irina; Bader, Marius; Wolf, Felix; Kulik, Andreas; Al-Dilaimi, Arwa; Wibberg, Daniel; Kalinowski, Jörn; Gross, Harald; Kaysser, Leonard
• Is Part Of: Chemical science. Volume 10:Issue 16(2019)
• Page Start: 4486
• Page End: 4490
• Publication Date: 2019-03-21
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c9sc00641a
• Languages: English
• ISSNs: 2041-6520

Abstract

Abstract : In the biosynthesis of phosphoramidon-like metalloprotease inhibitors three enzymes cooperate in the condensation of two amino acids and the subsequent attachment of a 6-deoxyhexose via a phosporamidate bridge. 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 thel -rhamnose moiety by phosphoester linkage.