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Ｎ－ａｃｙｌａｍｉｎｏａｃｉｄ ａｍｉｄｏ ｈｙｄｒｏｌａｓｅ（ＥＣ ３， ５， １， １４）是含锌金属酶，每摩 尔酶蛋白含两摩尔Ｚｎ２＋。本实验通过金属螯合剂ＥＤＴＡ对酶透析脱去酶中的锌离子， 生成不含金属离子的ａｐｏ－酶，再分别以 Ｍｎ２＋， Ｎｉ２＋离子对 ａｐｏ－酶重组，生成相 应的金属离子取代酶，研究了它们的活力与ｐＨ值的关系，热稳定性，游离的金属离子 对酶活性的影响，并通过荧光发射光谱考察了相应构象的变化。
N-acylaminoacid amido hydrolase (EC 3, 5, 1, 14) is a zinc-containing metalloenzyme containing two moles of Zn 2+ per mol of enzyme protein. In this experiment, the metal chelator EDTA was used to dialysis the enzyme to remove the zinc ion in the enzyme to generate the apo-enzyme without metal ion, and then recombine the apo-enzyme with Mn2 + and Ni2 + ions to generate the corresponding metal ion-substituted enzyme The relationship between their vitality and pH value, thermal stability and the effect of free metal ions on the enzyme activity were investigated. The corresponding conformational changes were investigated by fluorescence emission spectroscopy.