Biotin-dependent enzyme

Biotin-dependent enzymes are a family of enzymes that utilize the vitamin biotin as a covalently bound prosthetic group (cofactor) for catalyzing key metabolic reactions, primarily carboxylation, but also decarboxylation and transcarboxylation[1][4][5][6]. The most well-characterized members in humans are the carboxylases: acetyl-CoA carboxylase, propionyl-CoA carboxylase, pyruvate carboxylase, methylcrotonyl-CoA carboxylase, and (in some taxa) geranyl-CoA carboxylase[1][2][3]. These enzymes are essential for processes such as fatty acid synthesis, gluconeogenesis, branch-chain amino acid metabolism, and other anaplerotic pathways[2][3][5]. Structurally, they share a conserved biotin-binding domain that facilitates the transfer of a carboxyl group between substrates via a swinging-arm mechanism[4][5]. Biotin-dependent enzymes are ancient, with conserved domains across all domains of life[4]. In humans, their deficiency leads to serious metabolic disorders, often responsive to biotin supplementation. In addition to their metabolic roles, biotinylation of non-enzymatic proteins such as histones can affect gene expression and chromatin stability[1][2]. Key notes: - "Biotin-dependent enzymes" refers to a family, not a single entity; for disease or drug targeting, it is crucial to specify which member or deficiency is relevant[4][1]. - There are no canonical abbreviations for the family as a whole; individual enzymes have recognized abbreviations (e.g., ACC, PCC, PC, MCC)[1][3]. - Direct pharmacological modulation is limited to dietary supplementation; enzyme deficiencies are most relevant therapeutically[2].

Other names

Biotin-dependent carboxylaseBiotin enzyme familyAcyl-CoA carboxylase familyCarboxylase (biotin)Class I carboxylase

Cofactor supplementation (biotin restores activity of deficient biotin-dependent enzymes). No established small-molecule drugs directly modulate their activity in clinical practice.