Waser M R, Garfinkel L, Kohn M C, Garfinkel D
J Theor Biol. 1983 Jul 21;103(2):295-312. doi: 10.1016/0022-5193(83)90030-9.
The kinetics of the phosphofructokinase reaction were studied by computer modeling. A general random order, two-state allosteric model, of which the Monod--Wyman--Changeux model is a limiting case, was found to most accurately reproduce the experimental observations of Pettigrew & Frieden (1979 a,b). A simplified model with Hill coefficients was found to fit almost as well. In these models substrates bind preferentially to and stabilize the enzyme in the R state, and ATPH3-, the inhibitory species, binds preferentially to and stabilizes the enzyme in the T state. Enzymatic activity is regulated by conversion from the R to the T state, which is effected by protonation, especially of the uncomplexed enzyme, but the experimental data are inadequate for accurate estimation of the pKa of the enzyme. Random order binding of substrates is an important cause of sigmoidal kinetics. Additional experiments that would aid in the discrimination among rival models are described.
通过计算机建模研究了磷酸果糖激酶反应的动力学。发现一种一般随机顺序的双态别构模型（其中莫诺德 - 怀曼 - 尚热模型是一个极限情况）能最准确地重现佩蒂格鲁和弗里登（1979年a，b）的实验观察结果。发现一个具有希尔系数的简化模型拟合效果几乎同样好。在这些模型中，底物优先结合并稳定处于R态的酶，而抑制性物质ATPγ - 优先结合并稳定处于T态的酶。酶活性通过从R态向T态的转变来调节，这种转变受质子化影响，特别是未结合底物的酶的质子化，但实验数据不足以准确估计该酶的pKa。底物的随机顺序结合是S形动力学的一个重要原因。描述了有助于区分竞争模型的其他实验。
