Ekdahl K N, Ekman P
FEBS Lett. 1984 Feb 27;167(2):203-9. doi: 10.1016/0014-5793(84)80127-1.
Rat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated into unphosphorylated and fully phosphorylated enzyme. The effects of fructose 2,6-bisphosphate and AMP on these two enzyme forms were examined. Unphosphorylated fructose-1,6-bisphosphatase was more easily inhibited by both effectors. Fructose 2,6-bisphosphate affected both K0.5 and Vmax, while the main effect of AMP was to lower Vmax. Fructose 2,6-bisphosphate and AMP together acted synergistically to decrease the activity of fructose-1,6-bisphosphatase, and since unphosphorylated and phosphorylated enzyme forms are affected differently, this might be a way to amplify the effect of phosphorylation.
大鼠肝脏果糖-1,6-二磷酸酶在体外被部分磷酸化,并分离为未磷酸化和完全磷酸化的酶。研究了果糖2,6-二磷酸和AMP对这两种酶形式的影响。未磷酸化的果糖-1,6-二磷酸酶更容易受到这两种效应物的抑制。果糖2,6-二磷酸影响K0.5和Vmax,而AMP的主要作用是降低Vmax。果糖2,6-二磷酸和AMP共同协同作用降低果糖-1,6-二磷酸酶的活性,并且由于未磷酸化和磷酸化的酶形式受到不同的影响,这可能是一种放大磷酸化作用的方式。