Mathematical analysis of ligand-induced monomerization and dimerization in the monomer dimer equilibrium of proteins. Application to D-amino acid oxidase.
We have mathematically analyzed ligand-induced monomerization and dimerization in a protein monomer-dimer equilibrium system, in which the monomer has one and the dimer two binding sites. These dimer sites have the same binding constants for the first ligand but may cooperatively interact when one of them is occupied by a ligand molecule. In this system, the apparent dimerization constant and the apparent molecular weight are functions of free ligand concentration, and depend on the intrinsic binding constants of the ligand molecule to the monomer and the dimer. The behavior of these functions is classified into 17 cases according to the values of the three intrinsic binding constants, and some calculated examples are shown graphically for selected parameters. The theory was also applied to D-amino acid oxidase [EC 1.4.3.3], a flavoprotein, and the pH dependence of the apparent dimerization constant and the apparent molecular weight in the presence of ligand, p-aminobenzoate, were studied theoretically using parameters obtained in our previous experiments (5).
D010129:4-Aminobenzoic Acid / Q000378:metabolism*; D062365:Aminobenzoates / Q000378:metabolism*; D000818:Animals; D003605:D-Amino-Acid Oxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology; D046911:Macromolecular Substances; D008433:Mathematics; D008956:Models, Chemical; D008970:Molecular Weight; D011485:Protein Binding; D013552:Swine
D062365:Aminobenzoates; D046911:Macromolecular Substances; D003605:D-Amino-Acid Oxidase; D010129:4-Aminobenzoic Acid