BCAT2 Human

BCAT2 is a mitochondrial enzyme that catalyzes the first step in the catabolism of BCAAs. It converts these amino acids into their corresponding branched-chain alpha-keto acids while concurrently producing glutamate . The enzyme functions as a homodimer, consisting of two identical polypeptide chains. Each chain is composed of two domains: a small subunit (residues 1-170) and a large subunit (residues 182-365), connected by a short, looping region (residues 171-181) .

The active site of BCAT2 lies at the interface between the two domains and requires the cofactor pyridoxal-5’-phosphate (PLP) for activity. PLP forms a Schiff base linkage with a lysine residue of the enzyme, which is essential for the enzyme’s catalytic function .

BCAT2 is involved in the catabolic pathway of BCAAs, which are essential amino acids that must be obtained from the diet. The enzyme’s activity is crucial for maintaining the balance of these amino acids in the body. Disruptions in BCAT2 function can lead to metabolic disorders such as hypervalinemia and hyperleucine-isoleucinemia .

Recombinant human BCAT2 is produced using genetic engineering techniques. The BCAT2 gene is cloned into an expression vector, which is then introduced into a host organism, typically Escherichia coli or yeast. The host cells express the BCAT2 protein, which is subsequently purified through various chromatographic techniques to obtain the recombinant enzyme .

Recombinant BCAT2 is used in various research applications to study the metabolism of BCAAs and their role in health and disease. It is also utilized in the development of therapeutic strategies for metabolic disorders involving BCAAs .