STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE .I. STRUCTURAL SYMMETRY AND CONFORMATIONAL CHANGES
STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE .I. STRUCTURAL SYMMETRY AND CONFORMATIONAL CHANGES
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DOI：
10.1016/0003-9861(65)90037-8
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发表时间：
1965-01-01
影响因子：
3.9
通讯作者：
BRANDEN, CI
中科院分区：
文献类型：
--
作者：
BRANDEN, CI
本文介绍了马肝醇脱氢酶晶体的x射线初步研究，以及该酶及其辅酶和某些抑制剂之间形成的各种二元和三元配合物。游离酶及其与辅酶的复合物分子含有两个相同的亚基，每个亚基的分子量约为42000，它们通过双对称轴相互联系。抑制剂分子如吡唑和异丁酰胺诱导酶分子的构象变化。
The paper describes a preliminary X-ray investigation of crystals of horse-liver alcohol dehydrogenase and various binary and ternary complexes formed between this enzyme, its coenzyme, and some inhibitors. Molecules of free enzyme and its complex with coenzyme contain two identical subunits, each of molecular weight approximately 42.000, which are related by a twofold symmetry axis. Inhibitor molecules like pyrazole and iso-butyramide induce conformational changes in the enzyme molecule.