Supramolecular organization of glycolytic enzymes.
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.
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
D009097:Multienzyme Complexes; D010732:Phosphofructokinase-1; D006597:Fructose-Bisphosphatase