InterPro domain: IPR033939

Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leucine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two forms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme [ 1 ]. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism [ 2 ]. Members of this entry are widely distributed in all three forms of life.

1. Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Biochim. Biophys. Acta 1647, 61-5
2. Structure and function of branched chain aminotransferases. Prog. Nucleic Acid Res. Mol. Biol. 70, 175-206