PCCA (propionyl-CoA carboxylase subunit alpha) is the catalytic alpha subunit of the biotin-dependent mitochondrial enzyme propionyl-CoA carboxylase (PCC). This enzyme catalyzes the ATP-dependent carboxylation of biotin, which is subsequently transferred to propionyl-CoA to form methylmalonyl-CoA 1. PCCA functions in the catabolism of odd-chain fatty acids, branched-chain amino acids (isoleucine, threonine, methionine, valine), and other metabolites 1. The enzyme also acts on alternative substrates including butyryl-CoA at lower rates. Propionyl-CoA carboxylase is essential for feeding propionyl-CoA into the tricarboxylic acid cycle for energy metabolism 1. Mutations in PCCA cause propionic acidemia (PA), a genetic metabolic disorder characterized by impaired propionyl-CoA conversion and subsequent accumulation of propionyl-CoA and its metabolites 1. This accumulation leads to life-threatening complications including cardiac diseases and metabolic dysfunction through mitochondrial energy impairment and oxidative stress induction 1. Recent evidence demonstrates that PCCA activity can be enhanced by isoflavone biochanin-A binding, which promotes protective glutathione synthesis and ameliorates acetaminophen-induced liver injury 2. Reduced PCCA expression has been documented in liver failure patients, highlighting its clinical significance in hepatic function 2.