Nash P, McFadden G, Whitty A
Department of Biochemistry, University of Alberta, Edmonton, Canada.
FEBS Lett. 2000 Jun 9;475(1):1-6. doi: 10.1016/s0014-5793(00)01620-3.
Linear free energy relationships can be used to link the changes in rate constant for a reaction to changes in the equilibrium caused by alterations in structure. While they have most often been used in the analysis of chemical reactions, they have also been employed to resolve questions in enzymology and protein folding. Here we analyze the reaction of a serpin with a panel of six serine proteinases, and observe that a linear free energy relationship exists between the true second-order rate constant for reaction, k(inh), and the inhibition constant, K(I), indicating that formation of the covalent serpin-enzyme complex may be reversible.
线性自由能关系可用于将反应速率常数的变化与结构改变引起的平衡变化联系起来。虽然它们最常用于化学反应分析，但也被用于解决酶学和蛋白质折叠方面的问题。在这里，我们分析了一种丝氨酸蛋白酶抑制剂（serpin）与一组六种丝氨酸蛋白酶的反应，并观察观察观察应的真实二级速率常数k(inh)与抑制常数K(I)之间存在线性自由能关系，这表明共价丝氨酸蛋白酶抑制剂 - 酶复合物的形成可能是可逆的。
