1509-92-8

Basic information

• Product Name: N-Acetyl-D-methionine
• Synonyms: (R)-2-acetaMido-4-(Methylthio)butanoic acid;Acetyl-D-methionine≥ 99% (HPLC);n-acetyl-d-methioninecrystalline;ACETYL-D-METHIONINE;AC-D-METHIONINE;AC-D-MET-OH;N-ALPHA-ACETYL-D-METHIONINE;N-ACETYL-D-MET
• CAS NO: 1509-92-8
• Molecular Formula: C₇H₁₃NO₃S
• Molecular Weight: 191.25
• EINECS: 216-144-4
• Product Categories: amino;Pharmaceutical intermediates;Amino ACIDS SERIES;Amino Acid Derivatives;Amino Acids;Methionine [Met, M];A - H;Amino Acids;Modified Amino Acids
• Mol File: 1509-92-8.mol

Chemical Properties

• Melting Point: 103-106 °C
• Boiling Point: 453.6 °C at 760 mmHg
• Flash Point: 228.1 °C
• Appearance: White/Crystalline
• Density: 1.202 g/cm³
• Vapor Pressure: 1.72E-09mmHg at 25°C
• Refractive Index: 1.51
• Storage Temp.: −20°C
• PKA: 3.50±0.10(Predicted)
• BRN: 1725553
• CAS DataBase Reference: N-Acetyl-D-methionine(CAS DataBase Reference)
• NIST Chemistry Reference: N-Acetyl-D-methionine(1509-92-8)
• EPA Substance Registry System: N-Acetyl-D-methionine(1509-92-8)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36
• WGK Germany: 3
• Hazardous Substances Data: 1509-92-8(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
N-Acetyl-D-methionine is used as an active pharmaceutical ingredient for its potential therapeutic effects. It may play a role in various medical applications due to its unique structure and properties.
Used in Nutritional Supplements:
N-Acetyl-D-methionine is used as a dietary supplement for its potential health benefits. It may contribute to the maintenance of healthy bodily functions and support overall well-being.
Used in Cosmetics Industry:
N-Acetyl-D-methionine is used as an ingredient in the cosmetics industry for its potential skin health benefits. It may be included in skincare products to promote skin health and improve overall skin appearance.
Used in Research and Development:
N-Acetyl-D-methionine is used as a research compound for its potential applications in various scientific studies. It may be utilized to explore new therapeutic approaches and understand its effects on biological systems.

Synthesis Reference(s)

Journal of the American Chemical Society, 73, p. 4604, 1951 DOI: 10.1021/ja01154a030

InChI:InChI=1/C7H13NO3S/c1-5(9)8-6(7(10)11)3-4-12-2/h6H,3-4H2,1-2H3,(H,8,9)(H,10,11)/t6-/m1/s1

Upstream product

• 348-67-4 D-methionine 
• 108-24-7 acetic anhydride 
• 1115-47-5 N-acetyl-DL-methionine 
• 60-35-5 acetamide 
• 3268-49-3 3-(methylsulfenyl)propanal 
• 201230-82-2 carbon monoxide 
• 21691-49-6 D-methionine methyl ester 
• 10332-17-9 DL-methionine methyl ester 
• 55585-92-7 N-acetyl-homocysteine 

Downstream Products

• 348-67-4 D-methionine 

Relevant articles and documents

An improved racemase/acylase biotransformation for the preparation of enantiomerically pure amino acids

Using directed evolution, a variant N-acetyl amino acid racemase (NAAAR G291D/F323Y) has been developed with up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids. The variant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic resolution which allows 98% conversion of N-acetyl-dl-allylglycine into d-allylglycine in 18 h at high substrate concentrations (50 g L-1). This is the first example of NAAAR operating under conditions which would allow it to be successfully used on an industrial scale for the production of enantiomerically pure α-amino acids. X-ray crystal analysis of the improved NAAAR variant allowed a comparison with the wild-type enzyme. We postulate that a network of novel interactions that result from the introduction of the two side chains is the source of improved catalytic performance.

An environmentally benign and selective electrochemical oxidation of sulfides and thiols in a continuous-flow microreactor

A practical and environmentally benign electrochemical oxidation of thioethers and thiols in a commercially-available continuous-flow microreactor is presented. Water is used as the source of oxygen to enable the oxidation process. The oxidation reaction utilizes the same reagents in all scenarios and the selectivity is solely governed by the applied potential. The procedure exhibits a broad scope and good functional group compatibility providing access to various sulfoxides (15 examples), sulfones (15 examples) and disulfides (6 examples). The use of continuous flow allows the optimal reaction parameters (e.g. residence time, applied voltage) to be rapidly assessed, to avoid mass- and heat-transfer limitations and to scale the electrochemistry.

Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; Exceptional features

Various commercial lyophilized and immobilized preparations of lipase A from Candida antarctica (CAL-A) were studied for their ability to catalyze the hydrolysis of amide bonds in N-acylated α-amino acids, 3-butanamidobutanoic acid (β-amino acid) and its ethyl ester. The activity toward amide bonds is highly untypical of lipases, despite the close mechanistic analogy to amidases which normally catalyze the corresponding reactions. Most CAL-A preparations cleaved amide bonds of various substrates with high enantioselectivity, although high variations in substrate selectivity and catalytic rates were detected. The possible role of contaminant protein species on the hydrolytic activity toward these bonds was studied by fractionation and analysis of the commercial lyophilized preparation of CAL-A (Cat#ICR-112, Codexis). In addition to minor impurities, two equally abundant proteins were detected, migrating on SDS-PAGE a few kDa apart around the calculated size of CAL-A. Based on peptide fragment analysis and sequence comparison both bands shared substantial sequence coverage with CAL-A. However, peptides at the C-terminal end constituting a motile domain described as an active-site flap were not identified in the smaller fragment. Separated gel filtration fractions of the two forms of CAL-A both catalyzed the amide bond hydrolysis of ethyl 3-butanamidobutanoate as well as the N-acylation of methyl pipecolinate. Hydrolytic activity towards N-acetylmethionine was, however, solely confined to the fractions containing the truncated form of CAL-A. These fractions were also found to contain a trace enzyme impurity identified in sequence analysis as a serine carboxypeptidase. The possible role of catalytic impurities versus the function of CAL-A in amide bond hydrolysis is further discussed in the paper. The Royal Society of Chemistry 2010.

Heat-stable D-aminoacylase

The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective, the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Efficient chemoenzymatic synthesis of enantiomerically pure α-amino acids

A general two-step chemoenzymatic synthesis for enantiomerically pure natural and nonnatural α-amino acids is presented. In the first step of the sequence, the ubiquitous educts aldehyde, amide and carbon monoxide react by palladium-catalyzed amidocarbonylation to afford the racemic N-acyl amino acids in excellent yields. In the second step, enzymatic enantioselective hydrolysis yields the free optically pure a-amino acid and the other enantiomer as the N-acyl derivative, both in optical purities of 85-99.5% ee. The advantage of the chemoenzymatic process compared to other amino acid synthesis are demonstrated by the preparation of various functionalized (-OR, -Cl, -F, -SR) α-amino acids on a 10-g scale.

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.

Efficient Asymmetric Hydrogenations of (Z)-2-Acetamidoacrylic Acid Derivatives with the Cationic Rhodium Complex of (2S,4S)-MOD-BPPM

The preparation of (2S,4S)-MOD-BPPM ((2S,4S)-N-(t-butoxycarbonyl)-4-phosphino>-2-phosphino>methyl>pyrrolidine) and its application to highly effective asymmetric hydrogenations of (Z)-2-acetamidoacrylic acid derivatives are described.

Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I

Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occuring α-amino acids.Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis.Eleven α-amino and α-methyl α-amino acids were resolved on a 2-29-g scale.Crude L- and D-amino acid products had generally >90percent ee.The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.