BCAT2 (branched chain amino acid transaminase 2) catalyzes the transamination of essential branched-chain amino acids (leucine, isoleucine, and valine) to their corresponding α-keto acids, initiating BCAA catabolism 1. This enzymatic activity occurs predominantly in skeletal muscle and is critical for producing acetyl-CoA and other metabolic intermediates that fuel cellular energy production and biosynthesis 21. Mechanistically, BCAT2-mediated BCAA catabolism sustains mitochondrial respiration and enhances BCAA uptake 2. In cancer contexts, BCAT2 upregulation reprograms BCAA metabolism to support tumor development and survival 3. Notably, BCAT2 interacts with PCBP1 to activate PI3K/AKT signaling, promoting cell proliferation while inhibiting autophagy-related apoptosis and ferroptosis 4. Clinically, BCAT2 dysregulation associates with multiple malignancies. Elevated BCAT2 expression correlates with aggressive phenotypes in pancreatic ductal adenocarcinoma, where KRAS-mediated stabilization of BCAT2 drives neoplasia progression 2. Similarly, BCAT2 is upregulated in hepatocellular carcinoma induced by aflatoxin B1 5, acute myeloid leukemia where METTL16-dependent upregulation promotes leukemia stem cell self-renewal 3, and nasopharyngeal carcinoma with therapeutic resistance 6. BCAT2 inhibition or dietary BCAA restriction shows promise in limiting tumor development, suggesting therapeutic potential across multiple cancer types.