Biotin-dependent enzymes are enzymes that use covalently attached biotin to transfer a carboxyl group during catalysis. The biotin cofactor is linked to a lysine residue within a carrier region of the protein and moves between distinct catalytic sites [1]. In biotin-dependent carboxylases, one site uses ATP and bicarbonate to carboxylate biotin, and another transfers the carboxyl group to an organic acceptor [2]. Domain movements carry this activated intermediate between the sites; in multimeric enzymes, the participating sites can lie on different polypeptide chains [3][4]. The holoenzyme can distribute biotin carboxylase, carrier, and carboxyltransferase functions among separate subunits. Their assembly positions the mobile biotin-bearing domain for successive reactions and links cofactor movement to substrate-specific carbon–carbon bond formation [5].
- biotinylation
- carboxylases
- biotin protein ligase
- covalent cofactor
Biotin and Related Studies·Cell Biology·Biochemistry, Genetics and Molecular Biology·Life Sciences
References
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