无机焦磷酸的酶催化水解。当前关于与碱性磷酸酶（EC 3.1.3.1）相关的PP1-磷酸水解活性表征问题的观点。
Enzyme catalyzed hydrolysis of inorganic pyrophosphate. Current view of problems in characterization of PP1-phosphohydrolytic activity associated with alkaline phosphatases (EC 3.1.3.1).
作者信息
HøRDER M
出版信息
Enzyme. 1975;19(3):165-91.
A survey of the hydrolytic activity of alkaline phosphatase (EC 3.1.3.1) reveals that PP1, like phosphomonoesters, can serve as substrate in vitro. This pp1-phosphohydrolytic activity can be distinguished from PP1-phosphohydrolytic activities of inorganic pyrophosphatases (EC 3.6.1.1) and glucose-6-phosphatase (EC 3.1.3.9) by several criteria. Discrimination among these hydrolytic enzymes is possible by their dependence on variation of pH and of magnesium to PP1 ratios in the assay solutions. The true substrates and modifiers are not simply PP1 and magnesium, but the equilibrium species in mixtures of these two. The physiological significance of each of the three enzymes is not predictable from their differential efficiency as catalysts of PP1-hydrolysis in vitro.
一项关于碱性磷酸酶（EC 3.1.3.1）水解活性的研究表明，PP1与磷酸单酯一样，在体外可作为底物。这种PP1 - 磷酸水解活性可通过几个标准与无机焦磷酸酶（EC 3.6.1.1）和葡萄糖 - 6 - 磷酸酶（EC 3.1.3.9）的PP1 - 磷酸水解活性区分开来。通过它们对测定溶液中pH值变化以及镁与PP1比例变化的依赖性，可以区分这些水解酶。真正的底物和调节剂不仅仅是PP1和镁，而是这两者混合物中的平衡物种。这三种酶各自的生理意义无法从它们在体外作为PP1水解催化剂的不同效率来预测。
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