Branched-chain amino acid aminotransferase, mitochondrial (BCAT2)

Branched-chain amino acid aminotransferase, mitochondrial (BCAT2), is a pyridoxal 5’-phosphate-dependent enzyme encoded by the *BCAT2* gene in humans. It catalyzes the reversible transamination of the essential branched-chain amino acids leucine, isoleucine, and valine, producing their respective alpha-ketoacids and glutamate[1][2]. BCAT2 functions in the mitochondria of most tissues and plays a crucial role in nitrogen transfer, metabolic regulation, and energy production; its activity is involved in glucose homeostasis, amino acid catabolism, and cellular redox maintenance[1][2][3]. Dysregulation of BCAT2 is implicated in several cancers and metabolic disorders, and its expression can be used as a biomarker for sensitivity to therapies inducing ferroptosis, a form of cell death relevant to cancer treatment[3]. BCAT2’s broad role and tissue distribution pose safety and therapeutic challenges for drug targeting, as its disruption may lead to essential metabolic imbalances.

Other names

BCAT2BCATMBCT2ECA40PP18BCAMBCATmPlacental protein 18branched chain amino-acid transaminase 2HVLI

Inhibitors (including RNA interference, small molecules) block expression or function of BCAT2, leading to disruption of amino acid metabolism and induction of ferroptosis in cancer cells. Indirect modulation by compounds which induce or inhibit ferroptosis via AMPK/SREBP1 signaling, impacting BCAT2 transcription.