Nitrogenous group transferases, also known as transaminases or aminotransferases, are a class of enzymes that catalyze the transfer of a nitrogenous group, typically an amino group (–NH2), from one molecule to another. These enzymes are crucial in various biological processes, including amino acid metabolism, protein synthesis, and the production of neurotransmitters.
Nitrogenous group transferases primarily function by shuttling an amino group from an amino acid to an α-keto acid, forming a new amino acid and a new α-keto acid. This process, known as transamination, is a reversible reaction that is facilitated by the enzyme's cofactor, typically pyridoxal phosphate (PLP), which plays an essential role in the transfer of the amino group.
These enzymes play a vital role in converting one amino acid into another, allowing for the synthesis of different proteins and metabolic compounds. They are involved in maintaining the balance of amino acids in the body and also play a crucial role in the regulation of the levels of neurotransmitters like serotonin, dopamine, and glutamate.
Deficiencies or abnormalities in nitrogenous group transferases can lead to a variety of metabolic disorders, such as certain types of liver diseases or neurodegenerative disorders. The measurement of the activity of these enzymes in the blood can serve as diagnostic markers for specific diseases and conditions.
Overall, nitrogenous group transferases are essential enzymes involved in the interconversion of amino acids and crucial metabolic pathways within the human body.
