36357-77-4Relevant academic research and scientific papers
Biosynthetic reconstitution of deoxysugar phosphoramidate metalloprotease inhibitors using an N-P-bond-forming kinase
Baulig, Alexandra,Helmle, Irina,Bader, Marius,Wolf, Felix,Kulik, Andreas,Al-Dilaimi, Arwa,Wibberg, Daniel,Kalinowski, J?rn,Gross, Harald,Kaysser, Leonard
, p. 4486 - 4490 (2019)
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.
Synthesis of the endothelin converting enzyme inhibitor phosphoramidon
De Nanteuil, Guillaume,Benoist, Alain,Remond, Georges,Descombes, Jean-Jacques,Barou, Veronique,Verbeuren, Tony J.
, p. 1435 - 1438 (2007/10/02)
Phosphoramidon, an endothelin converting enzyme inhibitor, is synthesized by coupling of a rhamnose derivative with a dichlorophosphate and a suitably protected dipeptide.
