Biotin carboxylase (BC)

Biotin carboxylase is an essential enzyme component of all biotin-dependent carboxylases and catalyzes the ATP-dependent carboxylation of biotin, using bicarbonate as the CO₂ donor. It is highly conserved and functions within multi-component complexes, notably the acetyl-CoA carboxylase complex, which is critical for the first committed step in fatty acid biosynthesis. Biotin carboxylase works by activating and transferring a carboxyl group to biotin, which is then shuttled to a carboxyltransferase subunit to complete substrate carboxylation (e.g., of acetyl-CoA, propionyl-CoA). Its activity is vital for lipid, amino acid, and carbohydrate metabolism across all domains of life, and malfunctions or inhibition can disrupt central metabolic pathways. Due to its fundamental role in metabolic regulation, particularly in the acetyl-CoA carboxylase complex, biotin carboxylase is considered a therapeutic and agrochemical target for drug and herbicide development in contexts such as diabetes, cancer, obesity, and microbial infection[1][2][3][5][6].

Inhibition of fatty acid biosynthesis by blocking biotin-dependent carboxylation (for herbicides, antibiotics)