酵母乙醇脱氢酶中锌的状态与可及性
State and accessibility of zinic in yeast alcohol dehydrogenase.
作者信息
Leskovac V, Trivić S, Latkovska M
出版信息
Biochem J. 1976 Apr 1;155(1):155-61. doi: 10.1042/bj1550155.
Abstract
- Yeast alcohol dehydrogenase (EC 1.1.1.1) is inhibited in the presence of 1,10-phenanthroline. 2. A conformational change in the enzyme's structure is induced by 1,10-phenanthroline, and is abolished in the presence of NADH. 1,10-Phenanthroline binds to the enzyme competitively with respect to NADH, with a stoicheiometry of 2 mol of 1,10-phenanthroline/144000g of enzyme. 3. 1,10-Phenanthroline induces a time-dependent dissociation of Zn2+ from the enzyme, which is in correlation with its inhibitions. 4. Spectrophotometric measurement indicates that the dissociation of half (2 zinc atoms/tetramer) of the total zinc content of the enzyme correlates with the full inhibition of its activity. Measurement of the tightly bound Zn2+ by atomic absorption photometry confirms this. 5. A proposition is advanced that the tetrameric molecule of yeast alcohol dehydrogenase possesses an inherent asymmetry, with four monomeric subunits being arranged in two mutually symmetrical pairs.
摘要
- 酵母乙醇脱氢酶（EC 1.1.1.1）在1,10-菲咯啉存在时受到抑制。2. 1,10-菲咯啉可诱导该酶结构发生构象变化，而在烟酰胺腺嘌呤二核苷酸（NADH）存在时这种变化消失。1,10-菲咯啉相对于NADH与该酶竞争性结合，化学计量比为2摩尔1,10-菲咯啉/144000克酶。3. 1,10-菲咯啉可诱导锌离子（Zn2+）从该酶上发生时间依赖性解离，这与其抑制作用相关。4. 分光光度法测量表明，该酶总锌含量的一半（每四聚体2个锌原子）解离与酶活性的完全抑制相关。通过原子吸收光度法对紧密结合的Zn2+进行测量证实了这一点。5. 有人提出一个观点，即酵母乙醇脱氢酶的四聚体分子具有内在不对称性，四个单体亚基以两个相互对称的对排列。
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