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61193-04-2

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61193-04-2 Usage

Description

4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is a chemical compound that belongs to the class of piperidine derivatives. It is characterized by its chemical formula C10H10N2O2 and a molecular weight of 190.20 g/mol. 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is known for its complex structure and chemical properties, which necessitate careful handling and proper disposal to mitigate potential hazards to human health and the environment.

Uses

Used in Pharmaceutical Industry:
4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is utilized as a building block in the synthesis of various organic compounds, playing a crucial role in the development of new pharmaceutical products.
Used in Agrochemical Production:
4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile serves as an intermediate in the production of agrochemicals, contributing to the creation of substances that are vital for agricultural applications.
Used in Specialty Chemicals:
4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is also employed in the production of specialty chemicals, which are tailored for specific industries and applications.
Used in Medicinal Chemistry:
With its potential applications in medicinal chemistry, 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is instrumental in the research and development of innovative drugs, enhancing the scope of treatment options available in the medical field.

Check Digit Verification of cas no

The CAS Registry Mumber 61193-04-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,1,1,9 and 3 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 61193-04:
(7*6)+(6*1)+(5*1)+(4*9)+(3*3)+(2*0)+(1*4)=102
102 % 10 = 2
So 61193-04-2 is a valid CAS Registry Number.
InChI:InChI=1/C9H9N3O2/c1-9(2)5(3-10)7(13)12-8(14)6(9)4-11/h5-6H,1-2H3,(H,12,13,14)

61193-04-2SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name 4,4-dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile

1.2 Other means of identification

Product number -
Other names 4,4-dimethyl-2,6-dioxo-piperidine-3,5-dicarbonitrile

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:61193-04-2 SDS

61193-04-2Relevant articles and documents

The development of a new class of inhibitors for betaine-homocysteine S-methyltransferase

Pi?ha, Jan,Vaňek, Václav,Budě??sińsky, Milo?,Mlad?ková, Jana,Garrow, Timothy A.,Ji??acek, Ji??i

, p. 256 - 275 (2013/10/01)

Betaine-homocysteine S-methyltransferase (BHMT) is an important zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. In the liver, BHMT performs to half of the homocysteine remethylation. In this study, we systematically investigated the tolerance of the enzyme for modifications at the "homocysteine" part of the previously reported potent inhibitor (R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid (1). In the new compounds, which are S-alkylated homocysteine derivatives, we replaced the carboxylic group in the "homocysteine" part of inhibitor 1 with different isosteric moieties (tetrazole and oxadiazolone); we suppressed the carboxylic negative charge by amidations; we enhanced acidity by replacing the carboxylate with phosphonic or phosphinic acids; and we introduced pyrrolidine steric constraints. Some of these compounds display high affinity toward human BHMT and may be useful for further pharmacological studies of this enzyme. Although none of the new compounds were more potent inhibitors than the reference inhibitor 1, this study helped to completely defi ne the structural requirements of the active site of BHMT and revealed the remarkable selectivity of the enzyme for homocysteine.

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