82633-22-5Relevant articles and documents
Inhibitors of fumarylacetoacetate hydrolase domain containing protein 1 (Fahd1)
Eder, Manuel Philip,Gstach, Hubert,Jansen-Dürr, Pidder,Klapec, Patrycia,Liedl, Klaus R.,Loeffler, Johannes R.,Monteleone, Stefania,Weiss, Alexander K. H.,Wurzer, Richard,von Grafenstein, Susanne
, (2021/08/26)
FAH domain containing protein 1 (FAHD1) acts as oxaloacetate decarboxylase in mitochondria, contributing to the regulation of the tricarboxylic acid cycle. Guided by a high-resolution X-ray structure of FAHD1 liganded by oxalate, the enzymatic mechanism of substrate processing is analyzed in detail. Taking the chemical features of the FAHD1 substrate oxaloacetate into account, the potential inhibitor structures are deduced. The synthesis of drug-like scaffolds afforded first-generation FAHD1-inhibitors with activities in the low micromolar IC50 range. The investigations disclosed structures competing with the substrate for binding to the metal cofactor, as well as scaffolds, which may have a novel binding mode to FAHD1.
Oxidation of Enamine-esters with Lead Tetra-acetate. Part 2. Products from N-Aryl- and N-Benzyl-aminofumarates.
Vernon, John M.,Carr, Richard M.,Sukari, Mohamed A.
, p. 1310 - 1334 (2007/10/02)
Dimethyl anilinofumarate and N-benzylaminofumarate are oxidised by lead tetra-acetate to pyrroline, pyrrolin-2-one and pyrrole derivatives.Some other N-arylaminofumarates give the corresponding oxanilates by autoxidative cleavage.
