Kretschmer M, Schellenberger W, Hofmann E
Biochem Biophys Res Commun. 1985 Sep 16;131(2):899-904. doi: 10.1016/0006-291x(85)91324-5.
The cooperation of phosphofructokinase-2 and fructose-2,6-bisphosphatase is investigated. Experimentally derived rate laws of the kinase and bisphosphatase activities introduced into the respective differential equations permitted to describe the time evolution of fructose-2,6-bisphosphate to quasi-stationary levels. The two enzyme activities were found to exert strong temperature dependence. The quasi-stationary levels of fructose-2,6-bisphosphate, however, are independent on temperature.
研究了磷酸果糖激酶-2与果糖-2,6-二磷酸酶的协同作用。将通过实验得出的激酶和双磷酸酶活性速率定律引入各自的微分方程,可以描述果糖-2,6-二磷酸随时间演变为准稳态水平的过程。发现这两种酶活性具有很强的温度依赖性。然而,果糖-2,6-二磷酸的准稳态水平与温度无关。