Eklund H, Ramaswamy S, Plapp B V, el-Ahmad M, Danielsson O, Höög J O, Jörnvall H
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
EXS. 1994;71:269-77. doi: 10.1007/978-3-0348-7330-7_27.
The structures of horse liver alcohol dehydrogenase class I in its apoenzyme form and in different ternary complexes have been determined at high resolution. The complex with NAD+ and the substrate analogue pentafluorobenzyl alcohol gives a detailed picture of the interactions in an enzyme-substrate complex. The alcohol is bound to the zinc and positioned so that the hydrogen atom can be directly transferred to the C4 atom of the nicotinamide ring. The structure of cod liver alcohol dehydrogenase with hybrid properties (functionally of class I but structurally overall closer to class III) has been determined by molecular replacement methods to 3 A resolution. Yeast alcohol dehydrogenase has been crystallized, and native data have been collected to 3 A resolution.
已高分辨率测定了马肝乙醇脱氢酶I类的脱辅酶形式及不同三元复合物的结构。与NAD⁺和底物类似物五氟苄醇形成的复合物给出了酶-底物复合物中相互作用的详细情况。醇与锌结合并定位，使得氢原子可直接转移至烟酰胺环的C4原子。具有混合特性（功能上属于I类但整体结构更接近III类）的鳕鱼肝乙醇脱氢酶的结构已通过分子置换法测定至3 Å分辨率。酵母乙醇脱氢酶已结晶，且已收集到3 Å分辨率的天然数据。
