Biotin-dependent carboxylase enzyme

Biotin-dependent carboxylase enzymes are a family of enzymes that catalyze the biotin- and ATP-dependent carboxylation of various substrates, a reaction critical in pathways such as fatty acid, amino acid, and carbohydrate metabolism. They require a covalently attached biotin cofactor to shuttle activated CO~2~ (as carboxybiotin) between distinct enzyme active sites—typically a biotin carboxylase site and a carboxyltransferase site, often organized into multi-component or multi-domain complexes. Members of this enzyme family include acetyl-CoA carboxylase, propionyl-CoA carboxylase, pyruvate carboxylase, 3-methylcrotonyl-CoA carboxylase, and others. These enzymes are highly conserved and widely distributed in nature. Mutations in the genes encoding these enzymes cause a range of inborn errors of metabolism, and some isoforms are targeted by commercial herbicides and are viewed as potential therapeutic targets in diseases like type 2 diabetes, obesity, and cancer.

Other names

Biotin-dependent carboxylaseBiotin carboxylaseBC (for subunit/component)Biotin-dependent carboxylases (plural, but less specific)Component names: Acetyl-CoA carboxylase (ACC)Component names: Propionyl-CoA carboxylase (PCC)Component names: Pyruvate carboxylase (PC)Component names: 3-Methylcrotonyl-CoA carboxylase (MCC)Component names: Geranyl-CoA carboxylaseComponent names: Urea carboxylase (UC)

Inhibitors reduce the enzyme's ability to carboxylate substrates, impacting lipid, amino acid, or carbohydrate synthesis Some herbicides selectively inhibit the plastid form in plants, blocking fatty acid synthesis