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
References
- Moritz Hunkeler; Anna Hagmann; Edward Stuttfeld; Mohamed Chami; Yakir Guri; Henning Stahlberg; Timm Maier; Structural Basis for Regulation of Human Acetyl-CoA Carboxylase. Nature 2018, 558, 470-474, 10.1038/s41586-018-0201-4.
- Liang Tong; Structure and Function of Biotin-dependent Carboxylases. Cell. Mol. Life Sci. 2012, 70, 863-891, 10.1007/s00018-012-1096-0.
- Alejandro D. Meruelo; Seong Kyu Han; Sanguk Kim; James U. Bowie; Structural Differences Between Thermophilic and Mesophilic Membrane Proteins. Protein Sci. 2012, 21, 1746-1753, 10.1002/pro.2157.
- Martin St. Maurice; Laurie Reinhardt; Kathy H. Surinya; Paul V. Attwood; John C. Wallace; W. Wallace Cleland; Ivan Rayment; Domain Architecture of Pyruvate Carboxylase, a Biotin-Dependent Multifunctional Enzyme. Science 2007, 317, 1076-1079, 10.1126/science.1144504.
- Christine S. Huang; Kianoush Sadre-Bazzaz; Yang Shen; Binbin Deng; Z. Hong Zhou; Liang Tong; Crystal Structure of the α6β6 Holoenzyme of Propionyl-Coenzyme A Carboxylase. Nature 2010, 466, 1001-1005, 10.1038/nature09302.