Which amino acid is primarily deaminated during oxidative deamination?

The amino acid primarily deaminated during oxidative deamination is glutamic acid. This process is important in amino acid metabolism, particularly in the liver, where glutamic acid can be converted into α-ketoglutarate through the removal of its amino group. This reaction not only plays a critical role in the urea cycle, where excess nitrogen is eliminated from the body, but also assists in the regulation of nitrogen balance and energy metabolism in cells.

Glutamic acid is unique among amino acids as it is the primary amino donor for nitrogen metabolism and is involved in the transamination reactions that generate other amino acids. Its deamination is a key step in allowing amino acids to be utilized for energy production, especially during periods of fasting or intense exercise when carbohydrates may be limited.

In contrast, while other amino acids like aspartic acid, tyrosine, and proline can also undergo deamination, they do not participate in oxidative deamination to the extent that glutamic acid does. The significance of glutamic acid in nitrogen metabolism and its extensive involvement in key metabolic pathways underscores its primary role in oxidative deamination.