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Hydrolysis of the amino group of glutamine yielding glutamate and ammonium. Catalyzing enzyme: glutaminase (EC 3.5.1.2) 2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate. For the conversion of glutamate to α-ketoglutarate three different reactions are possible: Catalyzing enzymes: glutamate dehydrogenase (GlDH), EC ...
Other reactions may take place via GS. Competition between ammonium ion and water, their binding affinities, and the concentration of ammonium ion, influences glutamine synthesis and glutamine hydrolysis. Glutamine is formed if an ammonium ion attacks the acyl-phosphate intermediate, while glutamate is remade if water attacks the intermediate.
The ammonia produced in neurons is fixed into α-ketoglutarate by the glutamate-dehydrogenase reaction to form glutamate, then transaminated by alanine aminotransferase into lactate-derived pyruvate to form alanine, which is exported to astrocytes. In the astrocytes, this process is then reversed, and lactate is transported in the other direction.
Glutamate also plays an important role in the body's disposal of excess or waste nitrogen. Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase, [17] as follows: glutamate + H 2 O + NADP + → α-ketoglutarate + NADPH + NH 3 + H + Ammonia (as ammonium) is then excreted predominantly as urea, synthesised in ...
Glutamate synthase (also known as Glutamine oxoglutarate aminotransferase) is an enzyme and frequently abbreviated as GOGAT. This enzyme manufactures glutamate from glutamine and α-ketoglutarate , and thus along with glutamine synthetase (abbreviated GS) plays a central role in the regulation of nitrogen assimilation in photosynthetic ...
In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction. 2 L-glutamate + NAD + L-glutamine + 2-oxoglutarate + NADH + H + Glutamate synthase facilitates the ammonium assimilation pathway, which follows the enzymes, nitrite reductase and glutamine synthase. [1]
Ammonium hydroxide, 50 mg/mL ... It is a selective NMDA receptor antagonist that competitively inhibits the ligand (glutamate) binding site of NMDA receptors. [1]
Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant of about 1 mM), and therefore toxic levels of ammonia would have to be present ...