title: Supramolecular organization of glycolytic enzymes.
abstract: On the basis of the analysis of the data on adsorption of glycolytic enzymes to structural proteins of skeletal muscles and to the 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 the glycolytic enzymes complex adsorbed to a biological support has been proposed. The key role in the formation of 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 contains one tetrameric molecule of 6-phosphofructokinase and two molecules of each of other glycolytic enzymes. Hexokinase is not a part of the complex. The molecular mass of the multienzyme complex is about 2.6 X 10(6) daltons. The multienzyme complex has symmetry axis of second order. The formation of the multienzyme complex leads to the compartmentation of glycolytic process. The problem of integration of physico-chemical mechanisms of enzyme activity regulation (allosteric, dissociative and adsorptive mechanisms) is discussed.
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D006597:Fructose-Bisphosphatase / Q000378:metabolism; D006019:Glycolysis; D008322:Mammals; D008954:Models, Biological; D009097:Multienzyme Complexes; D009132:Muscles / Q000201:enzymology; D010732:Phosphofructokinase-1 / Q000378:metabolism
chemical_list: D009097:Multienzyme Complexes; D010732:Phosphofructokinase-1; D006597:Fructose-Bisphosphatase