Biotin carboxylase enzyme (BC)

Biotin carboxylase is a highly conserved enzyme domain central to the catalysis of biotin-dependent carboxylases such as acetyl-CoA carboxylase, propionyl-CoA carboxylase, pyruvate carboxylase, methylcrotonyl-CoA carboxylase, and urea carboxylase. This domain catalyzes the ATP-dependent carboxylation of biotin, a critical step in the transfer of carboxyl groups to various substrates as part of multi-domain enzyme complexes. Biotin carboxylase activity is essential for pathways including fatty acid biosynthesis, gluconeogenesis, amino acid metabolism, and others. As a drug target, its inhibition has therapeutic and agrochemical potential, especially via targeting the broader carboxylase complexes it is part of. Mutations or inhibition of these enzymes can have clinical significance in cancer, metabolic syndromes, congenital disorders, and infectious diseases.

Other names

Biotin-dependent carboxylase domainBC domain

Inhibition of the carboxylation reaction: Drugs/herbicides inhibit ATP-dependent carboxylation of biotin, blocking fatty acid biosynthesis or related pathways