由柠檬酸草酰乙酸裂解酶催化的反应平衡
THE EQUILIBRIUM OF THE REACTION CATALYSED BY CITRATE OXALOACETATE-LYASE.
作者信息
TATE S S, DATTA S P
出版信息
Biochem J. 1965 Feb;94(2):470-7. doi: 10.1042/bj0940470.
Abstract
- A method of preparation and purification of citrate oxaloacetate-lyase (EC 4.1.3.6) from Aerobacter aerogenes is described. 2. The equilibrium of this reaction has been determined at pH 8.4 and 25 degrees . It has been shown that K, i.e. [citrate(3-)]/[oxaloacetate(keto) (2-)][acetate (-)], is 3.08+/-0.72, but that K(app.), i.e. [total citrate]/[total oxaloacetate][total acetate], is markedly affected by the initial concentrations of the reactants and magnesium. 3. The free-energy change during the cleavage of citrate has been calculated and compared with data from other sources. 4. The free energy of hydrolysis of acetyl-CoA has been evaluated from the present data. 5. A detailed knowledge of the interactions of the reactants with metal ions has been shown to be important in the calculation of the equilibrium constant and related thermodynamic functions.
摘要
- 描述了一种从产气气杆菌中制备和纯化柠檬酸草酰乙酸裂解酶（EC 4.1.3.6）的方法。2. 该反应的平衡已在pH 8.4和25摄氏度下测定。结果表明，K，即[柠檬酸（3-）]/[草酰乙酸（酮式）（2-）][乙酸盐（-）]，为3.08±0.72，但K（app），即[总柠檬酸]/[总草酰乙酸][总乙酸盐]，受到反应物和镁的初始浓度的显著影响。3. 已计算出柠檬酸裂解过程中的自由能变化，并与其他来源的数据进行了比较。4. 已根据现有数据评估了乙酰辅酶A的水解自由能。5. 已表明对反应物与金属离子相互作用的详细了解在平衡常数和相关热力学函数的计算中很重要。
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