14121-56-3Relevant 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.
Synthesis, structural and biological studies of some oxamic acids and their CoII, NiIIand CuII metal complexes
Kumar, Devendra,Bhadauria, Anupama,Sharma
, p. 427 - 430 (2012/03/12)
Six new metal complexes of CoII, NlII and Cu II with N-(4-methoxyphenyl)oxamic acid and N-(4-carboxyphenyl)oxamic acid have been synthesized and characterized by elemental analyses, IR, 1H NMR and electronic spe
Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives
Cunliffe,Franklin,Hales,Hill
, p. 2652 - 2658 (2007/10/02)
N-Oxaloglycine (3) is an α-ketoglutarate (1) analogue that is a competitive inhibitor of prolyl 4-hydroxylase (EC 1.14.11.2). A study of the structure-activity relationships of some other oxalo derivatives shows that substitution on the glycine moiety mod
