肝脏磷酸果糖激酶的一种激活因子。
An activation factor of liver phosphofructokinase.
作者信息
Furuya E, Uyeda K
出版信息
Proc Natl Acad Sci U S A. 1980 Oct;77(10):5861-4. doi: 10.1073/pnas.77.10.5861.
Abstract
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.
摘要
肝脏中的纯磷酸果糖激酶（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。一种在纯化过程中从该酶中去除且能防止ATP对磷酸果糖激酶抑制作用的因子已被分离出来。通过在葡聚糖G-25上进行凝胶过滤显示，该因子可分解为分子量不同的三个组分。这些因子能克服ATP的抑制作用，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，可逆转ATP的抑制作用。有人提出，激活因子和AMP对磷酸果糖激酶的激活作用足以解释肝脏中的糖酵解通量。
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