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2492-75-3

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2492-75-3 Usage

Uses

2-Oxohexanoic Acid (cas# 2492-75-3) has been useful in a biological study that investigated the impact of glutathione on wines oxidative stability.

Definition

ChEBI: A straight-chain fatty acid consisting of hexanoic acid having an oxo group at position 2.

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)

2492-75-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-oxohexanoic acid

1.2 Other means of identification

Product number -
Other names 2-keto-n-caproic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:2492-75-3 SDS

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

-

, (2008/06/13)

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