2492-75-3 Usage
Description
2-Oxohexanoic acid, also known as a straight-chain fatty acid, is a compound consisting of hexanoic acid with an oxo group at position 2. It is characterized by its unique structure and properties, making it a versatile molecule for various applications.
Uses
Used in Biological Studies:
2-Oxohexanoic acid is used as a research compound for studying the impact of glutathione on the oxidative stability of wines. Its presence in these studies helps to understand the role of glutathione in wine chemistry and its influence on the overall quality and shelf life of the product.
Used in Pharmaceutical Industry:
2-Oxohexanoic acid is used as an intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows for the development of new drugs with potential therapeutic applications.
Used in Chemical Synthesis:
2-Oxohexanoic acid is used as a building block in the synthesis of various organic compounds, including specialty chemicals and materials. Its versatility in chemical reactions makes it a valuable component in the development of new products.
Used in Analytical Chemistry:
2-Oxohexanoic acid is used as a reference compound in analytical chemistry for the identification and quantification of similar compounds in complex mixtures. Its distinct properties enable accurate measurements and comparisons in various analytical techniques.
Check Digit Verification of cas no
The CAS Registry Mumber 2492-75-3 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,4,9 and 2 respectively; the second part has 2 digits, 7 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 2492-75:
(6*2)+(5*4)+(4*9)+(3*2)+(2*7)+(1*5)=93
93 % 10 = 3
So 2492-75-3 is a valid CAS Registry Number.
InChI:InChI=1/C6H10O3/c1-2-3-4-5(7)6(8)9/h2-4H2,1H3,(H,8,9)
2492-75-3Relevant articles and documents
Characterization of d-amino acid aminotransferase from Lactobacillus salivarius
Kobayashi, Jyumpei,Shimizu, Yasuhiro,Mutaguchi, Yuta,Doi, Katsumi,Ohshima, Toshihisa
, p. 15 - 22 (2013/10/22)
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.
Oxoalkanoic acid derivatives as inhibitors of angiotensin converting enzyme
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, (2008/06/13)
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