O'Fagain C, Butler B M, Mantle T J
Biochem J. 1983 Sep 1;213(3):603-7. doi: 10.1042/bj2130603.
The effect of pH on the kinetics of rat liver arylsulphatases A and B is very similar and shows that two groups with pK values of 4.4-4.5 and 5.7-5.8 are important for enzyme activity. Substrate binding has no effect on the group with a pK of 4.4-4.5; however, the pK of the second group is shifted to 7.1-7.5 in the enzyme-substrate complex. An analysis of the effect of pH on the Ki for sulphate inhibition suggests that HSO4-is the true product. A model is proposed that involves the two ionizing groups identified in the present study in a concerted general acid-base-catalysed mechanism.
pH对大鼠肝脏芳基硫酸酯酶A和B动力学的影响非常相似,表明两个pK值分别为4.4 - 4.5和5.7 - 5.8的基团对酶活性很重要。底物结合对pK为4.4 - 4.5的基团没有影响;然而,在酶 - 底物复合物中,第二个基团的pK值移至7.1 - 7.5。对pH对硫酸盐抑制的Ki影响的分析表明,HSO4-是真正的产物。提出了一个模型,该模型在协同的一般酸碱催化机制中涉及本研究中鉴定的两个电离基团。