7267-58-5 Usage
General Description
2-[(Carboxycarbonothioyl)amino]anisole, also known as 2[(4-Methoxyphenyl)amino]-2-oxoethylcarbamodithioic acid, is a chemical compound with the molecular formula C11H12N2O3S2. It is a substituted anisole derivative with a carboxycarbonothioylamino functional group. 2-[(Carboxycarbonothioyl)amino]anisole has been studied for its potential use as an antifungal agent, and as a corrosion inhibitor for steel and other metals. It is also used in the synthesis of other organic compounds. However, there is limited information available on its specific uses and properties, and further research is needed to fully understand its potential applications in various industries.
Check Digit Verification of cas no
The CAS Registry Mumber 7267-58-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,6 and 7 respectively; the second part has 2 digits, 5 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 7267-58:
(6*7)+(5*2)+(4*6)+(3*7)+(2*5)+(1*8)=115
115 % 10 = 5
So 7267-58-5 is a valid CAS Registry Number.
7267-58-5Relevant 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.