210910-25-1

Basic information

• Product Name: N-ACETYL-L-SELENOMETHIONIN
• Synonyms: N-ACETYL-L-SELENOMETHIONIN USP/EP/BP;Butanoic acid, 2-(acetylamino)-4-(methylseleno)-, (2S)-
• CAS NO: 210910-25-1
• Molecular Formula: C7H13NO3Se
• Molecular Weight: 238.1
• Mol File: 210910-25-1.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: N-ACETYL-L-SELENOMETHIONIN(CAS DataBase Reference)
• NIST Chemistry Reference: N-ACETYL-L-SELENOMETHIONIN(210910-25-1)
• EPA Substance Registry System: N-ACETYL-L-SELENOMETHIONIN(210910-25-1)

Safety Data

• Hazardous Substances Data: 210910-25-1(Hazardous Substances Data)

Upstream product

• 3211-76-5 Seleno-L-methionine 
• 108-24-7 acetic anhydride 
• 19220-93-0 pentafluorophenyl acetate 
• 2578-28-1 seleno-DL-methionine 

Relevant articles and documents

Carvacrol codrugs: A new approach in the antimicrobial plan

Objective: The increasing prevalence of antibiotic-resistant bacterial infections led to identify alternative strategies for a novel therapeutic approach. In this study, we synthesized ten carvacrol codrugs - obtained linking the carvacrol hydroxyl group

Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N- acetyl-L-cysteines

The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography, gel-filtration column chromatography, and hydrophobic interaction column chromatography. Acylase activity with NAC and N-acetyl-L- methionine (NAM), a known substrate for acylase I, as substrates coeluted during all chromatographic steps. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the protein was purified to near homogeneity and had a subunit M(r) of 43 000, which is identical with the M(r) of acylase I from porcine kidney and bovine liver. n-Butylmalonic acid was a slow-binding inhibitor of acylase I and inhibited the deacetylation of NAC with a K(i) of 192 ± 27 μM. These results show that acylase I catalyzes the deacetylation of NAC. The acylase I-catalyzed deacetylation of a range of S-alkyl-N- acetyl-L-cysteines, their carbon and oxygen analogues, and the selenium analogue of NAM was also studied with porcine kidney acylase I. The specific activity of the acylase I-catalyzed deacetylation of these substrates was related to their calculated molar volumes and log P values. The S-alkyl-N- acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents were good acylase I substrates, whereas the S-alkyl-N-acetyl-L-cysteines with long (>C3) and branched S-alkyl substituents were poor acylase I substrates. The carbon and oxygen analogues of S-methyl-N-acetyl-L-cysteine and the carbon analogue of S-ethyl-N-acetyl-L-cysteine were poor acylase I substrates, whereas the selenium analogue of NAM was a good acylase I substrate.

L-Methionine related 1-amino acids by acylase cleavage of their corresponding N-acetyl-DL-derivatives

Acylase I from Aspergillus oryzae is an even more useful enzyme than suggested so far. Besides standard amino acids such as L-Met, L-Val and L-Phe, a number of additional sulfur- and selenium-containing amino acids can be obtained at useful reaction rates and in very high enantiomeric purity by kinetic resolution of the respective N-acetyl-DL-amino acids.