1420-88-8

Basic information

• Product Name: N,S-DIACETYLCYSTEAMINE
• Synonyms: 1-DIACETYLCYSTEAMINE;2-ACETAMINOETHYL-THIOACETATE;S-[2-(ACETYLAMINO)ETHYL]ETHANETHIOATE;S-[2-(ACETYLAMINO)ETHYL]ETHANETHIONATE;N,S-DIACETYL-BETA-MERCAPTOETHYLAMINE;N,S-DIACETYLCYSTEAMINE;N-ACETYL-S-ACETYLCYSTEAMINE;Acetic acid, thio-, S-ester with N-(2-mercaptoethyl)acetamide
• CAS NO: 1420-88-8
• Molecular Formula: C₆H₁₁NO₂S
• Molecular Weight: 161.22
• EINECS: 215-821-1
• Mol File: 1420-88-8.mol
• Article Data: 10

Chemical Properties

• Melting Point: 29-31 °C(lit.)
• Boiling Point: 181-182 °C15 mm Hg(lit.)
• Flash Point: >230 °F
• Appearance: /solid
• Density: 1.140 (estimate)
• Vapor Pressure: 0.00042mmHg at 25°C
• Refractive Index: 1.5500 (estimate)
• Storage Temp.: −20°C
• CAS DataBase Reference: N,S-DIACETYLCYSTEAMINE(CAS DataBase Reference)
• NIST Chemistry Reference: N,S-DIACETYLCYSTEAMINE(1420-88-8)
• EPA Substance Registry System: N,S-DIACETYLCYSTEAMINE(1420-88-8)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• RTECS: AJ6865000
• F: 3-9-21
• Hazardous Substances Data: 1420-88-8(Hazardous Substances Data)

Usage

General Description

N,S-Diacetylcysteamine is a chemical compound with the formula C6H11NO3S. It is a derivative of cysteamine, a natural compound found in living organisms. N,S-Diacetylcysteamine has been studied for its potential therapeutic applications, particularly in the treatment of cystinosis, a rare genetic disorder characterized by the accumulation of cystine in the cells. It is known to possess antioxidant properties and has been investigated for its potential use in protecting against oxidative stress and inflammation. Additionally, N,S-Diacetylcysteamine has shown promise in inhibiting the growth of cancer cells, making it a potential candidate for further research in cancer therapy. Overall, N,S-Diacetylcysteamine has demonstrated potential therapeutic benefits and warrants further investigation in various medical applications.

InChI:InChI=1/C6H11NO2S/c1-5(8)7-3-4-10-6(2)9/h3-4H2,1-2H3,(H,7,8)

Upstream product

• 1190-73-4 2-(acetylamino)ethanethiol 
• 108-24-7 acetic anhydride 
• 638-44-8 N,N'-(dithiodiethylene)bisacetamide 
• 64-19-7 acetic acid 
• 156-57-0 2-mercaptoethylamine hydrochloride 
• 60-23-1 Cysteamine 
• 463-51-4 Ketene 

Downstream Products

• 23255-41-6 3-oxobutanoyl-N-acetylcysteamine thioester 
• 1119-49-9 N-butylacetamide 
• 1190-73-4 2-(acetylamino)ethanethiol 
• 64-17-5 ethanol 
• 64-19-7 acetic acid 

Relevant articles and documents

Substrate specificity in ketosynthase domains from trans-AT polyketide synthases

Branching out: The substrate specificity profiles for a range of ketosynthase (KS) domains from trans-AT PKSs are reported. Evidence is provided that a sterically demanding amino acid residue adjacent to the active-site Cys residue confers specificity towards non-β-methyl-branched substrates (see scheme). Copyright

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Structural and functional analysis of the loading acyltransferase from avermectin modular polyketide synthase

The loading acyltransferase (AT) domains of modular polyketide synthases (PKSs) control the choice of starter units incorporated into polyketides and are therefore attractive targets for the engineering of modular PKSs. Here, we report the structural and biochemical characterizations of the loading AT from avermectin modular PKS, which accepts more than 40 carboxylic acids as alternative starter units for the biosynthesis of a series of congeners. This first structural analysis of loading ATs from modular PKSs revealed the molecular basis for the relaxed substrate specificity. Residues important for substrate binding and discrimination were predicted by modeling a substrate into the active site. A mutant with altered specificity toward a panel of synthetic substrate mimics was generated by site-directed mutagenesis of the active site residues. The hydrolysis of the N-acetylcysteamine thioesters of racemic 2-methylbutyric acid confirmed the stereospecificity of the avermectin loading AT for an S configuration at the C-2 position of the substrate. Together, these results set the stage for region-specific modification of polyketides through active site engineering of loading AT domains of modular PKSs.