酵母乙醇脱氢酶底物结合位点中组氨酸和半胱氨酸残基的证据。
Evidence for a histidine and a cysteine residue in the substrate-binding site of yeast alcohol dehydrogenase.
作者信息
Leskovac V, Pavkov-Pericin D
出版信息
Biochem J. 1975 Mar;145(3):581-90. doi: 10.1042/bj1450581.
Abstract
- Yeast alcohol dehydrogenase (EC 1.1.1.1) is inhibited by stoicheiometric concentrations of diethyl pyrocarbonate. The inhibition is due to the acylation of a single histidine residue/monomer (mol.wt. 36000). 2. Alcohol dehydrogenase is also inhibited by stoicheiometric amounts of 5,5'-dithiobis-(2-nitrobenzoate), owing to the modification of a single cysteine residue/monomer. 3. Native alcohol dehydrogenase binds two molecules of reduced coenzyme/molecule of enzyme (mol.wt. 144000). 4. Modification of a single histidine residue/monomer by treatment with diethyl pyrocarbonate prevents the binding of acetamide in the ternary complex, enzyme-NADH-acetamede, but does not prevent the binding of NADH to the enzyme. 5. Modification of a single cysteine residue/monomer does not prevent the binding of acetamide to the ternary complex. After the modification of two thiol groups/monomer by treatment with 5,5'-dithiobis-(2-nitrobenzoate), the capacity of enzyme to bind coenzyme in the ternary complex was virtually abolished. 6. From the results presented in this paper we conclude that at least one histidine and one cysteine residue are closely associated in the substrate-binding site of alcohol dehydrogenase.
摘要
- 酵母乙醇脱氢酶（EC 1.1.1.1）会被化学计量浓度的焦碳酸二乙酯抑制。这种抑制作用是由于单个组氨酸残基/单体（分子量36000）被酰化。2. 乙醇脱氢酶也会被化学计量的5,5'-二硫代双（2-硝基苯甲酸）抑制，这是由于单个半胱氨酸残基/单体被修饰。3. 天然乙醇脱氢酶每个酶分子（分子量144000）结合两个还原型辅酶分子。4. 用焦碳酸二乙酯处理使单个组氨酸残基/单体发生修饰后，会阻止乙酰胺在酶-NADH-乙酰胺三元复合物中的结合，但不会阻止NADH与酶的结合。5. 单个半胱氨酸残基/单体的修饰不会阻止乙酰胺与三元复合物的结合。在用5,5'-二硫代双（2-硝基苯甲酸）处理使每个单体的两个巯基发生修饰后，酶在三元复合物中结合辅酶的能力几乎完全丧失。6. 根据本文给出的结果，我们得出结论：在乙醇脱氢酶的底物结合位点中，至少一个组氨酸残基和一个半胱氨酸残基紧密相关。
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