Gutowicz Jan, Terlecki Grzegorz
Department of Physico-chemistry of Microorganisms, Institute of Genetics and Microbiology, Przybyszewskiego 63/77, Wrocław University, Poland.
Cell Mol Biol Lett. 2003;8(3):667-80.
This article deals with the binding of glycolytic enzymes with membranous or protein subcellular structures. The representative papers of the last three decades dealing with this matter are reviewed. The studies evidencing the binding of some glycolytic enzymes to insoluble subcellular proteins and membranous structures are presented. It is currently generally accepted that the glycolytic enzymes work in some organisation. Such organisation undoubtedly plays a marked role, although still poorly known, in the regulation processes of glycolysis. From this review, the conclusion emerges that the regulatory ability of the binding of glycolytic enzymes to cellular membranes should be added to the list of well-known mechanisms of post-translational regulation of the glycolytic enzymes. Some of the results presented are the background for the hypothesis that planar phospholipid domains in/on the membrane surface are capable of functioning as binding sites for these enzymes. Such binding can modify the conformation state of the enzymes, which results in changes in their kinetic properties; thus, it may function as a regulator of catalytic activity
本文探讨糖酵解酶与膜性或蛋白质亚细胞结构的结合。回顾了过去三十年中关于此问题的代表性论文。展示了一些证明某些糖酵解酶与不溶性亚细胞蛋白质和膜性结构结合的研究。目前普遍认为糖酵解酶以某种组织形式发挥作用。这种组织形式在糖酵解的调节过程中无疑起着显著作用，尽管仍知之甚少。从这篇综述中可以得出结论，糖酵解酶与细胞膜结合的调节能力应被列入糖酵解酶翻译后调节的已知机制列表中。所呈现的一些结果为以下假设提供了背景：膜表面的平面磷脂结构域能够作为这些酶的结合位点。这种结合可以改变酶的构象状态，从而导致其动力学性质发生变化；因此，它可能作为催化活性的调节剂发挥作用
