7267-58-5Relevant academic research and scientific papers
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.
New approach to the synthesis of 2-carbamoylbenzothiazoles
Yarovenko, V. N.,Stoyanovich, F. M.,Zolotarskaya, O. Yu.,Chernoburova, E. I.,Zararzin, I. V.,Krayushkin, M. M.
, p. 144 - 147 (2007/10/03)
The reactions of substituted anilines with chloroacetamide and sulfur in the presence of triethylamine afforded monothiooxamides. When treated with K3Fe(CN)6, the latter underwent cyclization to form 2-carbamoyIbenzothiazoles. The reactions were accompanied by the formation of the corresponding thiooxanilic acids, which also underwent cyclization to form benzothiazole-2-carboxylic acids.
