Catalysis by yeast alcohol dehydrogenase.
Catalysis by yeast alcohol dehydrogenase.
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DOI：
10.1007/978-1-4684-5901-2_26
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发表时间：
1991
影响因子：
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通讯作者：
B. Plapp;A. Ganzhorn;R. Gould;D. Green;T. Jacobi;E. Warth;D. A. Kratzer
中科院分区：
文献类型：
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作者：
B. Plapp;A. Ganzhorn;R. Gould;D. Green;T. Jacobi;E. Warth;D. A. Kratzer
醇脱氢酶的结构和机理已被广泛研究（Bränden et al., 1975; Klinman, 1981; Pettersson, 1987）。几种三元配合物中的马肝酶的三维结构已经以高分辨率解决了（Eklund et al., 1981,1982）。已知来自11种动物、植物和真菌的22种以上NAD+依赖性醇脱氢酶的氨基酸序列。这些序列的比较提出了许多关于这些酶的结构-功能关系的问题。活性位点的氨基酸残基是如何参与催化的？底物特异性的基础是什么？在不同酶的进化过程中选择了什么？
The structure and mechanism of alcohol dehydrogenases have been extensively studied (Bränden et al., 1975; Klinman, 1981; Pettersson, 1987). The three-dimensional structures of the horse liver enzyme in several ternary complexes have been solved at high resolution (Eklund et al., 1981, 1982). Amino acid sequences for more than 22 NAD+-dependent alcohol dehydrogenases from 11 animal, plant and fungal species are known. Comparison of these sequences raises many questions about the structure-function relationships in these enzymes. How do the amino acid residues at the active site participate in catalysis? What is the basis of substrate specificity? What was selected for during the evolution of the different enzymes?