Final answer:
The reactions involving the side chains of asparagine and glutamine transforming into aspartate and glutamate are transamination reactions, catalyzed by transaminases and requiring pyridoxal phosphate.
Step-by-step explanation:
Transamination Reactions in Amino Acid Metabolism
The reactions that asparagine and glutamine participate in, where their side chains (which in asparagine and glutamine are amide groups) are converted to the carboxylic acids found in aspartate and glutamate, are known as transamination reactions. These transamination reactions involve the transfer of an amino group to a keto acid, such as pyruvate, oxaloacetate, or a-ketoglutarate, forming new keto acids and amino acids. The enzymes that catalyze these reactions are known as transaminases or aminotransferases and require pyridoxal phosphate as a coenzyme.
Transamination serves crucial functions in amino acid metabolism by allowing interconversion of amino acids and facilitating the channeling of amino groups to glutamate and aspartate, which is significant for many metabolic pathways, including the synthesis of purines and pyrimidines. Also, the reaction between glutamic acid and NAD catalyzed by glutamate dehydrogenase results in the production of a-ketoglutarate, NH3, and NADH, which highlights the role of glutamate in amino group metabolism.