An activation factor of liver phosphofructokinase.
An activation factor of liver phosphofructokinase.
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肝脏磷酸果糖激酶的激活因子。
DOI：
10.1073/pnas.77.10.5861
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发表时间：
1980
影响因子：
11.1
通讯作者：
Uyeda,K
中科院分区：
文献类型：
--
作者：
Furuya,E;Uyeda,K
来自肝脏的纯磷酸果糖激酶（ATP：D-果糖-6-磷酸1-磷酸转移酶，EC 2.7.1.11）受到 ATP 的强烈抑制，而粗制磷酸果糖激酶仅受到 ATP 的轻微抑制。已分离出一种因子，该因子在纯化过程中从酶中去除，并且可以阻止 ATP 对磷酸果糖激酶的抑制。如 Sephadex G-25 上的凝胶过滤所示，该因子可分解为分子量不同的三种成分。这些因素克服了 ATP 抑制，但在最佳测定条件下对催化活性没有影响。此外，AMP 与激活因子协同作用，逆转 ATP 抑制。有人提出，活化因子和 AMP 对磷酸果糖激酶的活化足以解释肝脏中的糖酵解通量。
Pure phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from liver is strongly inhibited by ATP, whereas crude phosphofructokinase is only slightly inhibited by ATP. A factor that is removed from the enzyme during purification and can prevent the inhibition of phosphofructokinase by ATP has been isolated. The factor can be resolved into three components that differ in molecular weights, as shown by gel filtration on Sephadex G-25. These factors overcome the ATP inhibition but have no effect on the catalytic activity under the optimum assay conditions. Furthermore, AMP acts syngeristically with the activation factor in reversing ATP inhibition. It is proposed that the activation of phosphofructokinase by the activation factor and AMP is sufficient to account for the glycolytic flux in the liver.