猪肝丙酮酸羧化酶。草酰乙酸脱羧反应途径。
Pig liver pyruvate carboxylase. The reaction pathway for the decarboxylation of oxaloacetate.
作者信息
Warren G B, Tipton K F
出版信息
Biochem J. 1974 May;139(2):321-9. doi: 10.1042/bj1390321.
Abstract
- The reaction pathway for the decarboxylation of oxaloacetate, catalysed by pig liver pyruvate carboxylase, was studied in the presence of saturating concentrations of K(+) and acetyl-CoA. 2. Free Mg(2+) binds to the enzyme in an equilibrium fashion and remains bound during all further catalytic cycles. MgADP(-) and P(i) bind randomly, at equilibrium, followed by the binding of oxaloacetate. Pyruvate is released before the ordered steay-state release of HCO(3) (-) and MgATP(2-). 3. These results are entirely consistent with studies on the carboxylation of pyruvate presented in the preceding paper (Warren & Tipton, 1974b) and together they allow a quantitative description of the reaction mechanism of pig liver pyruvate carboxylase. 4. In the absence of other substrates of the back reaction pig liver pyruvate carboxylase will decarboxylate oxaloacetate in a manner that is not inhibited by avidin. 5. Reciprocal plots involving oxaloacetate are non-linear curves, which suggest a negatively co-operative interaction between this substrate and the enzyme.
摘要
- 在饱和浓度的K⁺和乙酰辅酶A存在的情况下，研究了猪肝丙酮酸羧化酶催化草酰乙酸脱羧的反应途径。2. 游离的Mg²⁺以平衡方式与酶结合，并在所有后续催化循环中保持结合状态。MgADP⁻和磷酸根离子在平衡时随机结合，随后草酰乙酸结合。丙酮酸在HCO₃⁻和MgATP²⁻按顺序稳态释放之前释放。3. 这些结果与前文（沃伦和蒂普顿，1974b）中关于丙酮酸羧化的研究完全一致，它们共同使得对猪肝丙酮酸羧化酶的反应机制进行定量描述成为可能。4. 在不存在逆反应的其他底物的情况下，猪肝丙酮酸羧化酶将以不受抗生物素蛋白抑制的方式使草酰乙酸脱羧。5. 涉及草酰乙酸的双倒数图是非线性曲线，这表明该底物与酶之间存在负协同相互作用。
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本文引用的文献
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