22202-68-2

Usage

Uses

Used in Pharmaceutical Industry:
ALPHA-KETOGLUTARIC ACID MONOSODIUM SALT is used as a reagent for the human kynurenine amino transferase II (KAT II) inhibition spectra assay. This application is crucial in the research and development of drugs targeting KAT II, an enzyme involved in the breakdown of tryptophan, which is linked to various neurological and psychiatric disorders.
In the pharmaceutical industry, ALPHA-KETOGLUTARIC ACID MONOSODIUM SALT plays a significant role in the development of drugs that can potentially treat conditions related to the dysregulation of the kynurenine pathway. By serving as a reagent in the KAT II inhibition assay, it helps researchers understand the enzyme's function and develop targeted therapies for various diseases.
Additionally, ALPHA-KETOGLUTARIC ACID MONOSODIUM SALT may have other applications in different industries, such as in the field of biochemistry for studying metabolic pathways or in the development of diagnostic tools.

Biochem/physiol Actions

α-Ketoglutaric acid is the precursor for L-glutamic acid.

InChI:InChI=1/C5H6O5.Na/c6-3(5(9)10)1-2-4(7)8;/h1-2H2,(H,7,8)(H,9,10);/q;+1/p-2

Upstream product

• 142-47-2 monosodium L-glutamate 
• 21888-14-2 C₁₃H₁₇N₂O₉P 
• 328-50-7 α-ketoglutaric acid 

Downstream Products

• 617-65-2 Glutamic acid 
• 114-76-1 sodium phenylphyruvate 
• 108050-01-7 1-benzyl hydrogen 2-oxoglutarate 
• 876150-14-0 octyl α-ketoglutarate 
• 142-47-2 L-glutamic acid monosodium salt 

Relevant academic research and scientific papers

Chemical transformations of pyridoxal and pyridoxal 5′-phosphate condensation products with amino acids

The mechanism of chemical transformations of pyridoxal and pyridoxal 5′-phosphate condensation products with amino acids is studied by kinetic measurements. The Schiff bases are shown to be fairly stable in neutral media. In acid media, the Schiff bases a

ALPHA-KETOGLUTARATES AND THEIR USE AS THERAPEUTIC AGENTS

The present invention relates generally to the field of pharmaceuticals and medicine. More particularly, the present invention relates to certain compounds (e.g., α-ketoglutarate compounds; compounds that activate HIFα hydroxylase; compounds that increases the level of α ketoglutarate, etc.) and their use in medicine, for example, in the treatment of cancer (e.g., cancer in which the activity of one of the enzymes in the tricarboxylic acid (TCA) cycle is down regulated), in the treatment of angiogenesis (e.g., hypoxia-induced angiogenesis). One preferred class of compounds are α-ketoglutarate compounds having a hydrophobic moiety that is, or is part of, an ester group formed from one of the acid groups of α ketogluartic acid; and pharmaceutically acceptable salts, solvates, amides, esters, ethers, N oxides, chemically protected forms, and prodrugs thereof.

Some properties of glycine aminotransferase purified from Rhodopseudomonas palustris No. 7 concerning extracellular porphyrin production.

Glycine aminotransferase (EC 2.6.1.4; GlyAT) was presumed to be an enzyme concerning the supply of glycine for the extracellular porphyrin production by Rhodopseudomonas palustris No. 7. GlyAT was purified from strain No. 7 as an electrophoretically homogenous protein. The enzyme was a monomer protein with the molecular weight of about 42,000. From the absorption spectrum of the enzyme (350 nm, 410 nm), it was indicated that the enzyme had pyridoxal phosphate as a prosthetic group. The enzyme showed high substrate specificity for glutamate as an amino group donor. Apparent Kms for glutamate and glyoxylate were 6.20 mM and 3.75 mM, respectively. The Vmax and Kcat for glutamate were 66.8 mumol/min/mg protein and 46.8 s-1, respectively. The Vmax and Kcat for glyoxylate were 68.8 mumol/min/mg protein and 48.2 s-1. The optimum temperature and pH were 40-45 degrees C and 7.0-7.5, respectively. The enzyme activity lowered to about 50% in the presence of 15 mM ammonium chloride.