7558-63-6 Usage
Description
L-Glutamic Acid, Monoammonium Salt, also known as Monoammonium L-Glutamate, is a non-essential amino acid that serves as a primary excitatory neurotransmitter in the central nervous system (CNS). It is involved in synaptic transmission and plasticity, and its excessive release can lead to excitotoxicity associated with various neurological diseases. L-GLUTAMIC ACID, MONOAMMONIUM SALT is obtained by chemical synthesis and is characterized by its crystalline powder form, which is white, free-flowing, and odorless. It is soluble in water but insoluble in common organic solvents.
Uses
Used in the Food Industry:
L-Glutamic Acid, Monoammonium Salt is used as a flavor enhancer and salt substitute in the food industry. It is particularly useful in meats, soups, gravies, and sausage, providing a low sodium alternative to monosodium glutamate. This application takes advantage of its ability to enhance the taste of various food products while maintaining a healthy sodium content.
Used in Pharmaceutical Applications:
L-Glutamic Acid, Monoammonium Salt can protect hypertensive rats from strokes, making it a potential candidate for pharmaceutical applications related to stroke prevention and treatment in humans. Its role in this context is likely due to its involvement in neurotransmission and its ability to modulate excitotoxicity, which is a significant factor in stroke pathology.
Safety Profile
Moderately toxic by
intraperitoneal route. When heated to
decomposition it emits toxic fumes
including NOx and NH3.
Check Digit Verification of cas no
The CAS Registry Mumber 7558-63-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,5,5 and 8 respectively; the second part has 2 digits, 6 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 7558-63:
(6*7)+(5*5)+(4*5)+(3*8)+(2*6)+(1*3)=126
126 % 10 = 6
So 7558-63-6 is a valid CAS Registry Number.
InChI:InChI=1/C5H9NO4.2H3N/c6-3(5(9)10)1-2-4(7)8;;/h3H,1-2,6H2,(H,7,8)(H,9,10);2*1H3/t3-;;/m0../s1
7558-63-6Relevant articles and documents
Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris
Yoshimune, Kazuaki,Shirakihara, Yasuo,Wakayama, Mamoru,Yumoto, Isao
, p. 738 - 748 (2010)
Glutaminase from Micrococcus luteus K-3 [Micrococcus glutaminase (Mglu); 456 amino acid residues (aa); 48 kDa] is a salt-tolerant enzyme. Our previous study determined the structure of its major 42-kDa fragment. Here, using new crystallization conditions, we determined the structures of the intact enzyme in the presence and absence of its product L-glutamate and its activator Tris, which activates the enzyme by sixfold. With the exception of a 'lid' part (26-29 aa) and a few other short stretches, the structures were all very similar over the entire polypeptide chain. However, the presence of the ligands significantly reduced the length of the disordered regions: 41 aa in the unliganded structure (N), 21 aa for l-glutamate (G), 8 aa for Tris (T) and 6 aa for both l-glutamate and Tris (TG). l-Glutamate was identified in both the G and TG structures, whereas Tris was only identified in the TG structure. Comparison of the glutamate-binding site between Mglu and salt-labile glutaminase (YbgJ) from Bacillus subtilis showed significantly smaller structural changes of the protein part in Mglu. A comparison of the substrate-binding pocket of Mglu, which is highly specific for l-glutamine, with that of Erwinia carotovora asparaginase, which has substrates other than l-glutamine, shows that Mglu has a larger substrate-binding pocket that prevents the binding of l-asparagine with proper interactions.