583-92-6

Usage

Uses

Used in Pharmaceutical Industry:
4-methylsulfanyl-2-oxo-butanoic acid is used as an intermediate in the synthesis of various pharmaceutical compounds for its role in the metabolic pathway of L-methionine. It plays a crucial role in the production of essential amino acids and other biologically active molecules.
Used in Biochemical Research:
In the field of biochemical research, 4-methylsulfanyl-2-oxo-butanoic acid is utilized as a research tool to study the function and regulation of methionine transaminase, an enzyme involved in the conversion of L-methionine to 4-methylsulfanyl-2-oxo-butanoic acid. This helps in understanding the metabolic processes and potential therapeutic targets related to L-methionine metabolism.
Used in Nutritional Supplements:
4-methylsulfanyl-2-oxo-butanoic acid can be used as an additive in the development of nutritional supplements, particularly those aimed at supporting sulfur-containing amino acid metabolism and overall health.
Used in Food Industry:
In the food industry, 4-methylsulfanyl-2-oxo-butanoic acid may be employed as a flavor enhancer or a component in the production of additives that contribute to the taste and aroma of various food products. Its role in the metabolic pathway of L-methionine also makes it a potential candidate for applications related to the enhancement of protein quality in the food supply.

InChI:InChI=1/C5H8O3S/c1-9-3-2-4(6)5(7)8/h2-3H2,1H3,(H,7,8)

Upstream product

• 127-17-3 2-oxo-propionic acid 
• 59-51-8 DL-methionine 
• 328-50-7 α-ketoglutaric acid 
• 63-68-3 L-methionine 
• 348-67-4 D-methionine 

Downstream Products

• 63-68-3 L-methionine 
• 74-85-1 ethene 
• 348-67-4 D-methionine 
• 3268-49-3 3-(methylsulfenyl)propanal 
• 42537-72-4 N-methyl-L-methionine 
• 156-39-8 4-hydroxyphenylpiruvic acid 
• 74-93-1 methylthiol 
• 3387-85-7 2-(2,4-dinitro-phenylhydrazono)-4-methylsulfanyl-butyric acid 

Relevant academic research and scientific papers

Deracemization and Stereoinversion of α-Amino Acids by l-Amino Acid Deaminase

Enantiomerically pure α-amino acids are compounds of primary interest for the fine chemical, pharmaceutical, and agrochemical sectors. Amino acid oxidases are used for resolving d,l-amino acids in biocatalysis. We recently demonstrated that l-amino acid deaminase from Proteus myxofaciens (PmaLAAD) shows peculiar features for biotechnological applications, such as a high production level as soluble protein in Escherichia coli and a stable binding with the flavin cofactor. Since l-amino acid deaminases are membrane-bound enzymes, previous applications were mainly based on the use of cell-based methods. Now, taking advantage of the broad substrate specificity of PmaLAAD, a number of natural and synthetic l-amino acids were fully converted by the purified enzyme into the corresponding α-keto acids: the fastest conversion was obtained for 4-nitrophenylalanine. Analogously, starting from racemic solutions, the full resolution (ee >99%) was also achieved. Notably, d,l-1-naphthylalanine was resolved either into the d- or the l-enantiomer by using PmaLAAD or the d-amino acid oxidase variant having a glycine at position 213, respectively, and was fully deracemized when the two enzymes were used jointly. Moreover, the complete stereoinversion of l-4-nitrophenylalanine was achieved using PmaLAAD and a small molar excess of borane tert-butylamine complex. Taken together, recombinant PmaLAAD represents an l-specific amino acid deaminase suitable for producing the pure enantiomers of several natural and synthetic amino acids or the corresponding keto acids, compounds of biotechnological or pharmaceutical relevance. (Figure presented.).

Characterization of d-amino acid aminotransferase from Lactobacillus salivarius

We searched a UniProt database of lactic acid bacteria in an effort to identify d-amino acid metabolizing enzymes other than alanine racemase. We found a d-amino acid aminotransferase (d-AAT) homologous gene (UniProt ID: Q1WRM6) in the genome of Lactobacillus salivarius. The gene was then expressed in Escherichia coli, and its product exhibited transaminase activity between d-alanine and α-ketoglutarate. This is the first characterization of a d-AAT from a lactic acid bacterium. L. salivarius d-AAT is a homodimer that uses pyridoxal-5′-phosphate (PLP) as a cofactor; it contains 0.91 molecules of PLP per subunit. Maximum activity was seen at a temperature of 60 °C and a pH of 6.0. However, the enzyme lost no activity when incubated for 30 min at 30 °C and pH 5.5 to 9.5, and retained half its activity when incubated at pH 4.5 or 11.0 under the same conditions. Double reciprocal plots of the initial velocity and d-alanine concentrations in the presence of several fixed concentrations of α-ketoglutarate gave a series of parallel lines, which is consistent with a Ping-Pong mechanism. The Km values for d-alanine and α-ketoglutarate were 1.05 and 3.78 mM, respectively. With this enzyme, d-allo-isoleucine exhibited greater relative activity than d-alanine as the amino donor, while α-ketobutylate, glyoxylate and indole-3-pyruvate were all more preferable amino acceptors than α-ketoglutarate. The substrate specificity of L. salivarius d-AAT thus differs greatly from those of the other d-AATs so far reported.

Isolation, purification, and characterization of phenylpyruvate transaminating enzymes of Erwinia carotovora

Enzymes of Erwinia carotovora that transaminate phenylpyruvate were isolated, purified, and characterized. Two aromatic aminotransferases (PAT1 and PAT2) and an aspartic aminotransferase (PAT3) were found. According to gel filtration, these enzymes have molecular weights of 76, 75, and 78 kDa. The enzymes consist of two identical subunits of molecular weights of 31.4, 31, and 36.5 kDa, respectively. The isoelectric points of PAT1, PAT2, and PAT3 were determined as 3.6, 3.9, and 4.7, respectively. The enzyme preparations considerably differ in substrate specificity. All three of the enzymes productively interacted with the following amino acids: L-aspartic acid, L-leucine (except PAT3), L-isoleucine (except PAT3), L-serine, L-methionine, L-cysteine, L-phenylalanine, L-tyrosine, and L-tryptophane. The aromatic aminotransferases display higher specificity to the aromatic amino acids and the leucine-isoleucine pair, whereas the aspartic aminotransferase displays higher specificity to L-aspartic acid and relatively low specificity to the aromatic amino acids. The aspartic aminotransferase does not use L-leucine or L-isoleucine as a substrate. PAT1, PAT2, and PAT3 show the highest activity at pH 8.9 and at 48, 53, and 58°C, respectively.