492-27-3 Usage
Description
Kynurenic Acid, a product of L-Tryptophan metabolism, is a neuroactive compound with antiexcitotoxic and anticonvulsant properties. It plays a significant role in various physiological and pathological processes in the central nervous system.
Uses
Used in Pharmaceutical Applications:
Kynurenic Acid is used as a therapeutic agent for its antiexcitotoxic and anticonvulsant properties, making it a potential candidate for the treatment of neurological disorders and conditions involving excessive neuronal excitation.
Used in Research and Development:
Kynurenic Acid is used as a research tool in the study of neurotransmission and neurodegenerative diseases. It serves as an antagonist of NMDA and AMPA/kainate receptors, which are crucial for understanding the mechanisms underlying these conditions.
Used in Cell Culture Applications:
Kynurenic Acid is used as a constituent in dissection saline solution for embryonic cerebral cortical cells and human primary astrocytes. It helps maintain the integrity and functionality of these cells during experimental procedures.
Used in Cell Line Maintenance:
Kynurenic Acid is used as a medium supplement for murine intestinal epithelial cell line, MODE-K, and induced pluripotent stem cell (iPSC)-derived neurons cells. It supports the growth and differentiation of these cell types, contributing to the advancement of cell-based research and therapeutic applications.
Biological Activity
Broad spectrum EAA antagonist.
Biochem/physiol Actions
Kynurenic acid (KynA) is a non-selective antagonist of N-methyl-d-aspartate (NMDA), α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and kainate receptors. It blocks kainic acid neurotoxicity. Kynurenic acid also blocks nicotinic acetylcholine receptors. It is a by-product of tryptophan catabolic pathway. Kynurenic acid is a neuromodulator and controls the levels of glutamate, dopamine, acetylcholine and α-aminobutyric acid (GABA). KynA controls neuroendocrine functions and altered levels of KynA is a potential marker in depression, schizophrenia Alzheimer′s and Huntington′s diseases. Normal levels of KynA in the brain is crucial for the cognitive function.
Purification Methods
Crystallise the acid from absolute EtOH. The methyl ester crystallises from MeOH with m 224-226o. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p2723 1961, Beilstein 22 II 174, 22 III/IV 2245, 22/6 V 280.]
Check Digit Verification of cas no
The CAS Registry Mumber 492-27-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,9 and 2 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 492-27:
(5*4)+(4*9)+(3*2)+(2*2)+(1*7)=73
73 % 10 = 3
So 492-27-3 is a valid CAS Registry Number.
InChI:InChI=1/C10H7NO3.H2O/c12-9-5-8(10(13)14)11-7-4-2-1-3-6(7)9;/h1-5H,(H,11,12)(H,13,14);1H2
492-27-3Relevant articles and documents
Structural insight into the inhibition of human kynurenine aminotransferase I/Glutamine transaminase K
Han, Qian,Robinson, Howard,Cai, Tao,Tagle, Danilo A.,Li, Jianyong
, p. 2786 - 2793 (2009)
Human kynurenine aminotransferase I (hKAT I) catalyzes the formation of kynurenic acid, a neuroactive compound. Here, we report three high-resolution crystal structures (1.50-1.55 ?) of hKAT I that are in complex with glycerol and each of two inhibitors of hKAT I: indole-3-acetic acid (IAC) and Tris. Because Tris is able to occupy the substrate binding position, we speculate that this may be the basis for hKAT I inhibition. Furthermore, the hKAT/IAC complex structure reveals that the binding moieties of the inhibitor are its indole ring and a carboxyl group. Six chemicals with both binding moieties were tested for their ability to inhibit hKAT I activity; 3-indolepropionic acid and DL-indole-3-lactic acid demonstrated the highest level of inhibition, and as they cannot be considered as substrates of the enzyme, these two inhibitors are promising candidates for future study. Perhaps even more significantly, we report the discovery of two different ligands located simultaneously in the hKAT I active center for the first time.
Involvement of common intermediate 3-hydroxy-L-kynurenine in chromophore biosynthesis of quinomycin family antibiotics
Hirose, Yuki,Watanabe, Kenji,Minami, Atsushi,Nakamura, Takemichi,Oguri, Hiroki,Oikawa, Hideaki
experimental part, p. 117 - 122 (2012/01/31)
Quinomycin antibiotics, represented by echinomycin, are an important class of antitumor antibiotics. We have recently succeeded in identification of biosynthetic gene clusters of echinomycin and SW-163D, and have achieved heterologous production of echinomycin in Escherichia coli. In addition, we have engineered echinomycin non-ribosomal peptide synthetase to generate echinomycin derivatives. However, the biosynthetic pathways of intercalative chromophores quinoxaline-2-carboxylic acid (QXC) and 3-hydroxyquinaldic acid (HQA), which are important for biological activity, were not fully elucidated. Here, we report experiments involving incorporation of a putative advanced precursor, (2S, 3R)-6′- 2 H-3-hydroxy-L-kynurenine, and functional analysis of the enzymes Swb1 and Swb2 responsible for late-stage biosynthesis of HQA. On the basis of these experimental results, we propose biosynthetic pathways for both QXC and HQA through the common intermediate 3-hydroxy-L-kynurenine.
