Lavoinne A, Marchand J C, Chedeville A, Matray F
Biochimie. 1983 Mar;65(3):211-20. doi: 10.1016/s0300-9084(83)80086-8.
The kinetic properties of rat liver phosphoglycerate kinase were investigated in the forward direction of the reaction (utilization of ADP). The kinetic studies were performed in an assay system using combined hexokinase/glucose-6-phosphate dehydrogenase as an ATP trap. The Km values for Mg ADP1- and 1,3-diphospho-D-glycerate were approximately 0.11 and 0.006 mM, respectively. Reciprocal plots of 1/v versus 1/ (Mg ADP1-) at different fixed concentrations of 1,3-diphospho-D-glycerate and 1/v versus 1/ (1,3-diphospho-D-glycerate) at different fixed concentrations of Mg ADP1- were apparently parallel. However, product inhibition studies (3-phospho-D-glycerate), dead-end inhibition studies (2,3-diphospho-D-glycerate), and adenosine and AMP inhibition patterns yielded results consistent with a rapid equilibrium random mechanism in which the binding of one substrate greatly decreases the affinity of the enzyme for the second substrate. Existence of two sites for 3-phospho-D-glycerate is suggested.
研究了大鼠肝脏磷酸甘油酸激酶在反应正向（利用ADP）时的动力学特性。动力学研究是在一个使用己糖激酶/葡萄糖-6-磷酸脱氢酶组合作为ATP阱的测定系统中进行的。Mg ADP1-和1,3-二磷酸-D-甘油酸的Km值分别约为0.11和0.006 mM。在不同固定浓度的1,3-二磷酸-D-甘油酸下，1/v对1/（Mg ADP1-）的倒数作图，以及在不同固定浓度的Mg ADP1-下，1/v对1/（1,3-二磷酸-D-甘油酸）的倒数作图明显平行。然而，产物抑制研究（3-磷酸-D-甘油酸）、无效抑制研究（2,3-二磷酸-D-甘油酸）以及腺苷和AMP抑制模式得到的结果与快速平衡随机机制一致，即在该机制中一种底物的结合会大大降低酶对第二种底物的亲和力。提示存在两个3-磷酸-D-甘油酸结合位点。
