52809-07-1 Usage
Description
Quisqualic acid, also known as Quisqualate, is a naturally occurring amino acid derived from the fruits and seeds of Quisqualis chinensis. It functions as an agonist at multiple excitatory amino acid receptor substrates in the central nervous system, including high affinity for the kainate, AMPA, and metabotropic receptors. L-Quisqualic acid is an agonist of the neurotransmitter L-glutamate and is used to study receptor dynamics and as an excitotoxin.
Uses
Used in Neuroscience Research:
Quisqualic acid is used as a research tool for studying receptor dynamics in the central nervous system. It is particularly useful for differentiating between mGluR-1 and mGluR-4 receptors and for testing ligand-gated receptors in spiral ganglion neurons.
Used in Neurotransmission Studies:
As an agonist of L-glutamate, quisqualic acid is used to investigate the role of excitatory amino acid receptors in neurotransmission and synaptic plasticity.
Used in Neurodegenerative Disease Research:
L-Quisqualic acid serves as an excitotoxin and is used to selectively destroy neurons in the brain or spinal cord, which can help researchers understand the mechanisms underlying neurodegenerative diseases and develop potential therapeutic strategies.
Used in Drug Development:
Quisqualic acid's ability to modulate various receptor subtypes makes it a valuable compound in the development of drugs targeting the central nervous system, particularly for conditions involving excitatory amino acid receptor dysfunction.
Chemical Properties:
Quisqualic acid is an off-white solid with chemical properties that facilitate its use in various research and pharmaceutical applications.
Biological Activity
Glutamate receptor agonist acting at AMPA receptors and metabotropic glutamate receptors positively linked to phosphoinositide hydrolysis. Sensitizes neurons in hippocampus to depolarization by L-AP6 (the so called 'quis' effect). Also available as part of the Group I mGlu Receptor Tocriset? .
Biochem/physiol Actions
Active enantiomer of quisqualic acid; excitatory amino acid at glutamate receptors.
Purification Methods
It has been purified by ion-exchange chromatography on Dowex 50W (x 8, H+ form); the desired fractions are lyophilised and recrystallised from H2O/EtOH. It has IR (KBr) : 3400-2750br, 1830s, 1775s, 1745s and 1605s cm-1;maxand 1H NMR (NaOD/D2O, pH 13) : 3.55-3.57 (1H m, X of ABX, H-2), 3.72-3.85 (2H, AB of ABX, H-3), 1 3C NMR (D2O) : 50.1t, 53.4d, 154.8s, 159.7s and 171.3s. [Baldwin et al. J Chem Soc, Chem Commun 256 1985.] It is a quasiqualate receptor agonist [Joels et al. Proc Natl Acad Sci USA 86 3404 1989].
Check Digit Verification of cas no
The CAS Registry Mumber 52809-07-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,2,8,0 and 9 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 52809-07:
(7*5)+(6*2)+(5*8)+(4*0)+(3*9)+(2*0)+(1*7)=121
121 % 10 = 1
So 52809-07-1 is a valid CAS Registry Number.
InChI:InChI=1/C5H7N3O5/c6-2(3(9)10)1-8-4(11)7-5(12)13-8/h2H,1,6H2,(H,9,10)(H,7,11,12)/t2-/m0/s1
52809-07-1Relevant articles and documents
Syntheses of (S)-β-pyrazolylalanine and (S)-quisqualic acid from a serine-derived aziridine
Farthing, Christopher N.,Baldwin, Jack E.,Russell, Andrew T.,Schofield, Christopher J.,Spivey, Alan C.
, p. 5225 - 5226 (2007/10/03)
The naturally occurring amino acids (S)-β-pyrazolylalanine and (S)- quisqualic acid are synthesised via the nucleophilic ring-openings of an optically active aziridine by pyrazole and 1,2,4-oxadiazolidine-3,5-dione, respectively.
PURIFICATION AND PROPERTIES OF β-CYANO-L-ALANINE SYNTHASE FROM SPINACIA OLERACEA
Ikegami, Fumio,Takayama, Kyoko,Tajima, Chiho,Murakoshi, Isamu
, p. 2011 - 2016 (2007/10/02)
β-Cyano-L-alanine synthase was purified ca 6200-fold to homogeneity from the leaves of spinach (Spinacia oleracea).The purified enzyme has an apparent Mr of 60 000 and can be dissociated into identical subunits of Mr 30 000.The subunits each contain one molecule of pyridoxal 5'-phosphate.The Km value is 2.3 mM for L-cysteine and 0.73 mM for cyanide. β-Cyano-L-alanine synthase from S. oleracea also catalyses the formation of some S-substituted L-cysteines and some heterocyclic β-substituted alanines from L-cysteine or O-acetyl-L-serine.The specificity of these additional catalytic activities of the purified enzyme are compared with those of cysteine synthase purified from the same plant, and with those of β-cyano-L-alanine synthase purified from other sources.Some other properties, including the amino acid composition of the purified enzyme, are also described. - Key Word Index: Spinacia oleracea; Chenopodiaceae; spinach; β-cyano-L-alanine synthase; cysteine synthase; enzyme purification; amino acid composition; L-cysteine; O-acetyl-L-serine; β-cyano-L-alanine; heterocyclic β-substituted alanines.
ENZYMATIC SYNTHESIS OF THE NEUROEXCITATORY AMINO ACID QUISQUALIC ACID BY CYSTEINE SYNTHASE
Murakoshi, Isamu,Kaneko, Masakazu,Koide, Chiharu,Ikegami, Fumio
, p. 2759 - 2764 (2007/10/02)
Key Word Index - Quisqualis indica var. villosa; Combretaceae; cysteine synthase; isoenzyme; enzyme purification; biosynthesis; heterocyclic β-substituted alanines; quisqualic acid; O-acetyl-L-serine; cysteine.Purification of cysteine synthase from the leaves of Quisqualis indica var. villosa reveals the presence of two forms of this enzyme, separated by chromatography on DEAE-Sephadex A-50.Isoenzyme A was purified 10 000-fold and had a specific activity of 10.8 U/mg protein.Isoenzyme B was purified 460-fold with a specific activity of 0.49 U/mg protein.Both isoenzymes have the same Mrs (58 000) and dissociate into identical subunits (Mr 29 000).The Km value of isoenzyme A is 1.9 mM for O-acetyl-L-serine and 59 μM for sulphide, while that of isoenzyme B is 7.1 mM for O-acetyl-L-serine and 4.0 mM for 3,5-dioxo-1,2,4-oxadiazolidine.Both isoenzymes catalyse the formation of cysteine from O-acetyl-L-serine and hydrogen sulphide, but only isoenzyme B catalyses the formation of L-quisqualic acid.Other significant differences occur in the substrate specificity of the two isoenzymes.Some properties of the purified cysteine synthase isoenzymes are also described.
