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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 ...
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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.
In enzymology, a glutamate—tRNA ligase (EC 6.1.1.17) is an enzyme that catalyzes the chemical reaction. ATP + L-glutamate + tRNAGlu AMP + diphosphate + L-glutamyl-tRNAGlu. The 3 substrates of this enzyme are ATP, L-glutamate, and tRNA(Glu), whereas its 3 products are AMP, diphosphate, and L-glutamyl-tRNA(Glu).
Glutamate + ATP + NH 3 → Glutamine + ADP + phosphate Glutamine synthetase catalyzed reaction. Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. [4] The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. [5] Other reactions may take ...
In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction. L-glutamine + 2-oxoglutarate + NADPH + H + 2 L-glutamate + NADP + Thus, the four substrates of this enzyme are L-glutamine, 2-oxoglutarate (α-ketoglutarate), NADPH, and H +, whereas the two products are L-glutamate and NADP +.
While originally identified in a screen for organisms secreting L-glutamate, mutants of C. glutamicum have also been identified that produce various other amino acids and derivatives of amino acids. [6] Due to its industrial importance, several clones of C. glutamicum have been sequenced by both industry and academic groups. [5]