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7267-58-5

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7267-58-5 Usage

Compound type

Substituted anisole derivative

Functional group

Carboxycarbonothioylamino

Potential uses

Antifungal agent, corrosion inhibitor for steel and other metals, synthesis of other organic compounds

Availability of information

Limited

Need for further research

Yes

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.

7267-58-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-(2-methoxyanilino)-2-sulfanylideneacetic acid

1.2 Other means of identification

Product number -
Other names o-Methoxy-thio-oxanil-saeure

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:7267-58-5 SDS

7267-58-5Downstream Products

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.

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