Final answer:
The enzyme catalyzes oxidative deamination where L-glutamate is converted to a-ketoglutarate, accompanied by the removal and oxidation of an amino group, which forms ammonia and involves the conversion of NAD to NADH.
Step-by-step explanation:
The enzyme mentioned catalyzes a biochemical reaction known as oxidative deamination, in which L-glutamate is deaminated and oxidized to form a-ketoglutarate, releasing ammonia in the process. This is a key metabolic process that occurs mainly in the liver mitochondria.
The enzyme involved is glutamate dehydrogenase, an allosteric enzyme which is regulated by various molecules such as ATP, GTP, ADP, and NADH. The reduction of NAD to NADH also occurs during this reaction. In addition, glutamine synthetase is another important enzyme that catalyzes the conversion of glutamate and ammonia to glutamine, helping in ammonia detoxification.
Another related enzyme, malate dehydrogenase, is involved in the citric acid cycle, catalyzing the oxidation of malate to oxaloacetate. Transferases, a different class of enzymes, are involved in the transfer of functional groups between molecules—for instance, transaminases facilitate the exchange of amino groups between amino acids and keto acids, resulting in the formation of new compounds without the removal of hydrogen.
These biochemical pathways are crucial for energy production, waste removal, and the synthesis of various biomolecules in the body.