Final answer:
Transamination involves the transfer of an amino group from an amino acid to a keto acid, forming new amino and keto acids. Deamination is the removal of an amino group from amino acids, which can be oxidative or non-oxidative.
Step-by-step explanation:
Transamination is the transfer of an amino group from one amino acid to a keto acid, leading to the formation of a new keto acid and a new amino acid. Transamination reactions are catalyzed by transaminases or aminotransferases and require pyridoxal phosphate (PLP) as a coenzyme. These reactions are crucial in amino acid metabolism, and a common example includes the transfer of an amino group from an amino acid to alpha-ketoglutarate, forming glutamate.
Deamination, on the other hand, specifically involves the removal of an amino group from amino acids. There are two main types: oxidative deamination, wherein the amino group is removed following its oxidation (requires coenzymes such as FMN and FAD), and non-oxidative deamination, which occurs without oxidation. Oxidative deamination plays a role in the liver and kidneys, using amino acid oxidases.