Kurganov B I, Sugrobova N P, Mil'man L S
J Theor Biol. 1985 Oct 21;116(4):509-26. doi: 10.1016/s0022-5193(85)80086-2.
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.
基于对糖酵解酶与骨骼肌结构蛋白及红细胞膜吸附数据、酶 - 酶相互作用数据以及细胞代谢物对糖酵解酶活性调节数据的分析，提出了吸附于生物载体上的糖酵解酶复合物的结构。在多酶复合物形成过程中起关键作用的是6 - 磷酸果糖激酶。该酶分子有两个缔合位点，其中一个位点使6 - 磷酸果糖激酶固定在载体上，另一个位点被果糖 - 1,6 - 二磷酸醛缩酶饱和。多酶复合物包含一个6 - 磷酸果糖激酶四聚体分子以及其他每种糖酵解酶的两个分子。己糖激酶不是该复合物的一部分。多酶复合物的分子量约为2.6×10⁶道尔顿。多酶复合物具有二阶对称轴。多酶复合物的形成导致糖酵解过程的区室化。文中还讨论了酶活性调节的物理化学机制（别构、解离和吸附机制）的整合问题。
