与猪肾碱性磷酸酶相关的核苷焦磷酸酶活性
Nucleoside pyrophosphatase activity associated with pig kidney alkaline phosphatase.
作者信息
Wass M, Butterworth P J
出版信息
Biochem J. 1971 Oct;124(5):891-6. doi: 10.1042/bj1240891.
Abstract
- A study was made of the hydrolysis, at pH9.0, of ATP and ADP catalysed by pig kidney alkaline phosphatase. Both of these nucleoside pyrophosphates are substrates for the enzyme; K(m) values are 4x10(-5)m for ATP and 6.3x10(-5)m for ADP. V(max.) for ADP is approximately double that of ATP. 2. Above 0.1mm approximately, both ATP and ADP are inhibitory, but the inhibition is reversible by the addition of Mg(2+) ions to form MgATP(2-) or MgADP(-) complexes. The complexes, besides being non-inhibitory, are also substrates for the enzyme with K(m) values identical with those of the respective free nucleotides. 3. Mg(2+) ions are inhibitory when present in excess of ATP or ADP. The degree of inhibition is greater with ATP as substrate, but with both ATP and ADP a mixed competitive-non-competitive type of inhibition is observed. 4. It is suggested that under normal conditions the enzyme is inhibited by cellular concentrations of ATP plus ADP but that an increase in the concentration of Mg(2+) ions stimulates activity by relieving nucleoside pyrophosphate inhibition. The properties may be of importance in the regulation of the transport of bivalent cations.
摘要
- 对猪肾碱性磷酸酶在pH9.0条件下催化ATP和ADP水解进行了研究。这两种核苷焦磷酸都是该酶的底物；ATP的米氏常数（K(m)）为4×10⁻⁵m，ADP的米氏常数为6.3×10⁻⁵m。ADP的最大反应速度（V(max.)）约为ATP的两倍。2. 大约在0.1mm以上，ATP和ADP均具有抑制作用，但通过添加镁离子（Mg²⁺）形成MgATP²⁻或MgADP⁻复合物可使抑制作用逆转。这些复合物不仅无抑制作用，还是该酶的底物，其米氏常数与各自游离核苷酸的米氏常数相同。3. 当镁离子（Mg²⁺）的存在量超过ATP或ADP时具有抑制作用。以ATP作为底物时抑制程度更大，但以ATP和ADP作为底物时均观察到混合竞争性 - 非竞争性抑制类型。4. 有人提出，在正常条件下该酶受到细胞内ATP加ADP浓度的抑制，但镁离子（Mg²⁺）浓度的增加通过解除核苷焦磷酸的抑制作用来刺激活性。这些特性可能在二价阳离子转运的调节中具有重要意义。
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