61193-04-2

Basic information

• Product Name: 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile
• Synonyms: 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile;3-(R,S),5-(R,S)-3,5-dicyano-4,4-dimethyl-2,6-dioxopiperidine
• CAS NO: 61193-04-2
• Molecular Formula: C₉H₉N₃O₂
• Molecular Weight: 191.18666
• Mol File: 61193-04-2.mol
• Article Data: 2

Chemical Properties

• Melting Point: 212 °C
• Boiling Point: 484.8°C at 760 mmHg
• Flash Point: 247°C
• Appearance: /
• Density: 1.27g/cm³
• Vapor Pressure: 1.49E-09mmHg at 25°C
• Refractive Index: 1.516
• PKA: 16.75±0.70(Predicted)
• CAS DataBase Reference: 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile(CAS DataBase Reference)
• NIST Chemistry Reference: 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile(61193-04-2)
• EPA Substance Registry System: 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile(61193-04-2)

Safety Data

• Hazardous Substances Data: 61193-04-2(Hazardous Substances Data)

Usage

General Description

4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is a chemical compound that belongs to the class of piperidine derivatives. It has the chemical formula C10H10N2O2 and the molecular weight is 190.20 g/mol. 4,4-Dimethyl-2,6-dioxopiperidine-3,5-dicarbonitrile is used in the pharmaceutical industry as a building block for the synthesis of various organic compounds. It is also used as an intermediate in the production of agrochemicals and specialty chemicals. Additionally, it has potential applications in the field of medicinal chemistry for the development of new drugs. However, due to its complex structure and chemical properties, it requires careful handling and proper disposal to avoid any potential hazards to human health and the environment.

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)

Upstream product

• 110-89-4 piperidine 
• 7732-18-5 water 
• 67-64-1 acetone 
• 107-91-5 cyanoacetic acid amide 
• 105-56-6 ethyl 2-cyanoacetate 
• 759-58-0 ethyl isopropylidenecyanoacetate 

Downstream Products

• 22791-80-6 4,4-dimethyl-tetrahydro-pyran-2-one 
• 4160-82-1 3,3-dimethylglutaric anhydride 
• 53120-74-4 3,3-dimethylpent-1,5-diol 
• 91004-47-6 2,4-Dioxo-6,6-dimethyl-3-azabicyclo<3.1.0>hexan-1,5-dicarbonsaeure 
• 90868-50-1 2,4-Dioxo-5-carboxamido-6,6-dimethyl-3-azabicyclo<3.1.0>hexan-1-carbonsaeure 
• 100620-05-1 2,2,4-trimethyl-cyclohexane-1,1,3,3-tetracarboxylic acid 
• 22748-16-9 4,4-dimethylcyclopent-2-ene-1-one 
• 17804-59-0 diethyl 3,3-dimethylglutarate 
• 90961-45-8 N,N-di-n-butyl-9,9-dimethyl-3,7-diaza bicyclo-(3,3,1)-nonane 
• 90961-84-5 3,7-Dibutyl-9,9-dimethyl-3,7-diaza-bicyclo[3.3.1]nonane-2,4,6,8-tetraone 
• 4839-46-7 3,3-Dimethylglutaric acid 
• 5512-95-8 6,6-dimethyl-2,4-dioxo-3-aza-bicyclo[3.1.0]hexane-1,5-dicarbonitrile 

Relevant articles and documents

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

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.