Essential amino acid transamination

Transamination of essential amino acids refers to the enzymatic process where an amino group from an *essential amino acid* (such as valine, leucine, isoleucine, lysine, etc.) is transferred to an α-keto acid, forming a new amino acid and a new keto acid. This reaction is catalyzed by aminotransferase (transaminase) enzymes, which require pyridoxal phosphate (vitamin B6) as a cofactor. While most amino acids (both essential and non-essential) undergo transamination as part of their metabolism, transamination is especially important for synthesizing non-essential amino acids and for the catabolism of amino acids. The process is fundamental to nitrogen balance and the biosynthetic and degradative pathways of amino acids. Specific aminotransferases (such as ALT and AST) are widely used as clinical biomarkers for liver health. Because "essential amino acid transamination" describes a class of biochemical reactions catalyzed by multiple enzymes rather than a unique molecular target or receptor, it is not itself a therapeutic target[1][3][4].

Other names

Transamination of essential amino acidsAminotransferase reaction (for essential amino acids)Aminotransferase-mediated transamination

Transfer of amino group from an essential amino acid to an α-keto acid, catalyzed by aminotransferase/transaminase enzymes, requiring pyridoxal phosphate (PLP; active form of vitamin B6) as a coenzyme[1][2]