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应用底物反应动力学的方法进一步研究了去辅基的氨基酰化酶与锌重组复活的动力学机制以及高浓度的锌对酶活性和酶-ANS荧光复合物荧光性质的影响。实验结果表明:氨基酰化酶上至少有3个锌的结合部位,其中一个为紧结合部位,并为酶分子表现生物活性所必需,另外两个为比较松散的结合部位,其结合会影响酶的活性、酶分子的构象以及去辅基酶的复活动力学。两个松散的锌的结合部位不仅可以结合游离锌离子,并且可以结合zn(Ⅱ)-NTA复合物。
The reaction kinetics of substrate-assisted reaction was used to further study the kinetic mechanism of azoacylase and zinc recombination resuscitation and the effect of high concentrations of zinc on the enzymatic activity and the fluorescence properties of enzyme-AN fluorescence complexes. The experimental results show that there are at least three zinc binding sites on the aminoacylase, one of which is a tight binding site and is necessary for the enzyme molecule to exhibit biological activity. The other two are relatively loose binding sites, and the combination will affect the enzyme The conformation of the enzyme molecule and the revitalization kinetics of the decoyase. The two loose zinc binding sites bind not only free zinc ions but also zn (II) -NTA complexes.