[Supramolecular organization of glycolytic enzymes].
On the basis of the analysis of the data on adsorption of glycolytic enzymes to structural proteins of skeletal muscle and to erythrocyte membranes, the data on enzyme-enzyme interactions and the data on the regulation of activity of glycolytic enzymes by cellular metabolites the structure of glycolytic enzyme complex adsorbed to a biological support has been proposed. The key role in the formation of the multienzyme complex belongs to 6-phosphofructokinase. The enzyme molecule has two association sites, one of which provides the fixation of 6-phosphofructokinase on the support and another is saturated by fructose-1,6-bisphosphate aldolase. The multienzyme complex fixed on structural proteins of skeletal muscle contains one tetrameric molecule of 6-phosphofructokinase and at two molecules of other glycolytic enzymes. Hexokinase is not involved in the complex composition. The molecular mass of the multienzyme complex is about 2,6 X 10(6) Da. The formation of the multienzyme complex leads to the compartmentation of the glycolytic process. The problem of integration of physico-chemical mechanisms of enzyme activity regulation (allosteric, dissociative and adsorptive mechanisms) is discussed.
D000818:Animals; D002384:Catalysis; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006019:Glycolysis; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000378:metabolism
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D010732:Phosphofructokinase-1
Nadmolekuliarnaia organizatsiia fermentov glikoliza.