7558-63-6 Usage
Description
Different sources of media describe the Description of 7558-63-6 differently. You can refer to the following data:
1. Refer to monosodium glutamate.
2. L-Glutamic acid is a non-essential amino acid and the primary excitatory neurotransmitter in the CNS. It acts on ionotropic and metabotropic receptors to induce excitatory synaptic transmission and has roles in synaptic plasticity. Excessive release of L-glutamic acid induces excitotoxicity that is associated with various human diseases, including amyotrophic lateral sclerosis (ALS), stroke, Parkinson’s disease, Alzheimer’s disease, and Huntington’s disease. Excessive L-glutamic acid release, in its protonated glutamate form, also occurs during seizure activity and contributes to epileptogenesis and seizure-induced brain damage.
Uses
Different sources of media describe the Uses of 7558-63-6 differently. You can refer to the following data:
1. L-Glutamic Acid Monoammonium Salt is a food additive; It can protect hypertensive rats from strokes.
2. Monoammonium l-Glutamate is a flavor enhancer and salt substitute that is crystalline powder (white, free-flowing) and odorless. It is soluble in water, insoluble in common organic solvents, and is obtained by chemical synthesis. It is a low sodium alternative to monosodium glutamate. It is used in meats, soups, gravies, and sausage. It is also termed ammonium glutamate and monoammonium glutamate.
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.
