组氨酸残基与猪心上清液苹果酸脱氢酶的酶活性
Histidine residues and the enzyme activity of pig heart supernatant malate dehydrogenase.
作者信息
Holbrook J J, Lodola A, Illsley N P
出版信息
Biochem J. 1974 Jun;139(3):797-800. doi: 10.1042/bj1390797.
Abstract
- Supernatant pig heart malate dehydrogenase is completely inhibited by reaction with diethyl pyrocarbonate at pH6.5, when 0.58+/-0.1 residue of ethoxycarbonylhistidine is formed per NADH-binding site. 2. Oxaloacetate and hydroxymalonate protect the enzyme from inhibition in the absence of coenzyme. 3. Limited ethoxycarbonylation does not alter the binding of NADH to the enzyme but prevents the enzyme-NADH complex from interacting with hydroxymalonate in a ternary complex.
摘要
- 当每个NADH结合位点形成0.58±0.1个乙氧羰基组氨酸残基时，上清液猪心苹果酸脱氢酶在pH6.5下与焦碳酸二乙酯反应会被完全抑制。2. 在没有辅酶的情况下，草酰乙酸和羟基丙二酸可保护该酶不被抑制。3. 有限的乙氧羰基化不会改变NADH与该酶的结合，但会阻止酶-NADH复合物在三元复合物中与羟基丙二酸相互作用。
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本文引用的文献
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Structural studies of pig heart malate dehydrogenase.猪心苹果酸脱氢酶的结构研究。
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Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with alpha-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4.蛋白质的乙氧基甲酰化。在pH值为4的条件下，乙氧基甲酸酐与α-胰凝乳蛋白酶、胃蛋白酶和胰腺核糖核酸酶的反应。
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