title: [Kinetic model of the action of oligomeric enzymes using phosphofructokinase as an example. II. General formulation of the hierarchical model].
abstract: A general approach is suggested to describe the steady-state kinetics of the oligomeric enzymes on the base of the generalized statistical Ising model. Detailed analysis is given for the case of a oligomeric enzyme with a hierarchical supramolecular organization. A protomer of this enzyme composed of several equivalent subunits represents the quarternary level of structure. In their turn the finite or infinite number of protomers is associated into a oligomer thus creating a new "quinternary" level of the enzyme organization. The model accounts for the ligand-induced homotrophic cooperative interactions: firstly, between the neighbouring protomers and secondly, between the subunits of the same protomer. The influence of protomer conformation on the subunit state and the cooperativity induction caused by two-ligand binding are also taken into consideration. Monod-Wyman-Changeux's and Koshland's models are shown to be special limit cases of the suggested general theory.
authors.forename: D A
authors.initials: DA
authors.lastname: Cherepanov
mesh_terms: D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D004798:Enzymes; D046911:Macromolecular Substances; D010732:Phosphofructokinase-1
vernacular_title: Modelirovanie kinetiki deĭstviia oligomernykh fermentov na primere fosfofruktokinazy. II. Obshchaia formulirovka ierarkhicheskoĭ modeli.