Vanni A, Anfossi L, Pessione E, Giovannoli C
Dipartimento di Chimica Analitica, Università di Torino, V. Giuria 5, 10125 Turin, Italy.
Int J Biol Macromol. 2002 Mar 8;30(1):41-5. doi: 10.1016/s0141-8130(01)00188-x.
Yeast alcohol dehydrogenase (Y-ADH) is widely studied for its biotechnological importance and various attempts to improve its catalytic properties have been made. In this paper, a catalytically active metal-substituted Y-ADH was prepared in vitro by substituting one zinc atom with copper. EPR and Raman spectroscopy suggest that copper maintains the same co-ordination geometry as zinc in native Y-ADH. The active Cu-ADH shows lower substrate affinity and lower specific activity (SA) than native ADH, but greater than a previously obtained Co-ADH. Furthermore, Cu-ADH maintains its catalytic efficiency in a wider pH range than native enzyme.
酵母乙醇脱氢酶（Y-ADH）因其在生物技术方面的重要性而受到广泛研究，人们已进行了各种尝试来改善其催化性能。在本文中，通过用铜取代一个锌原子，在体外制备了具有催化活性的金属取代Y-ADH。电子顺磁共振（EPR）和拉曼光谱表明，铜在天然Y-ADH中保持与锌相同的配位几何结构。活性铜取代的乙醇脱氢酶（Cu-ADH）与天然乙醇脱氢酶相比，显示出较低的底物亲和力和较低的比活性（SA），但高于先前获得的钴取代的乙醇脱氢酶（Co-ADH）。此外，Cu-ADH在比天然酶更宽的pH范围内保持其催化效率。
