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Glutamic acid (symbol Glu or E; [4] the anionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins.It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use.
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Glutamate is a very major constituent of a wide variety of proteins; consequently it is one of the most abundant amino acids in the human body. [1] Glutamate is formally classified as a non-essential amino acid, because it can be synthesized (in sufficient quantities for health) from α-ketoglutaric acid, which is produced as part of the citric acid cycle by a series of reactions whose ...
Further research into the compound has found that only the L-glutamate enantiomer has flavor-enhancing properties. [3] Manufactured monosodium glutamate consists to over 99.6% of the naturally predominant L-glutamate form, which is a higher proportion of L-glutamate than can be found in the free glutamate ions of fermented naturally occurring ...
L-glutamate D-glutamate Hence, this enzyme RacE has one substrate , L-glutamate , and one product , D-glutamate. This enzyme belongs to the family of isomerases , specifically those racemases and epimerases acting on amino acids and derivatives, including proline racemase, aspartate racemase, and diaminopimelate epimerase. [ 1 ]
In biochemistry, the glutamate–glutamine cycle is a cyclic metabolic pathway which maintains an adequate supply of the neurotransmitter glutamate in the central nervous system. [1]
In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction L-glutamate + O 2 + H 2 O ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH 3 + H 2 O 2 The 3 substrates of this enzyme are L-glutamate , O 2 , and H 2 O , whereas its 3 products are 2-oxoglutarate , NH 3 , and H 2 O 2 .
L-arogenate + 2-oxoglutarate prephenate + L-glutamate Thus, the two substrates of this enzyme are L-arogenate and 2-oxoglutarate , whereas its two products are prephenate and L-glutamate . However, in most plant species utilizing this enzyme, the left side of the reaction is strongly favored.