glutamate dehydrogenase [NAD(P)+] activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+. [EC:1.4.1.3]

Glutamate dehydrogenase [NAD(P)+] activity is a crucial metabolic process catalyzed by the enzyme glutamate dehydrogenase. This enzyme facilitates the reversible interconversion of glutamate and α-ketoglutarate, a key intermediate in the citric acid cycle. The reaction involves the oxidation of glutamate to α-ketoglutarate, coupled with the reduction of NAD(P)+ to NAD(P)H. Conversely, α-ketoglutarate can be reduced to glutamate using NAD(P)H as a reducing agent. Glutamate dehydrogenase plays a vital role in nitrogen metabolism, connecting amino acid metabolism with the central metabolic pathways. It acts as a key regulatory enzyme in the synthesis and degradation of glutamate, the major amino acid involved in nitrogen transport and assimilation. Specifically, glutamate dehydrogenase serves to assimilate ammonia into glutamate, facilitating nitrogen incorporation into organic compounds. The enzyme's activity is influenced by various factors, including the concentration of substrates, coenzymes, and allosteric effectors. For instance, ADP and GTP act as allosteric inhibitors and activators, respectively, influencing the enzyme's activity to modulate the balance between glutamate synthesis and degradation. In summary, glutamate dehydrogenase [NAD(P)+] activity is a crucial enzymatic reaction responsible for the interconversion of glutamate and α-ketoglutarate, playing a central role in nitrogen metabolism and connecting amino acid metabolism with the central metabolic pathways.'
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Proteins (1)

Compounds (3)