Ozeki T, Mitsui Y, Sugiya H, Furuyama S
Department of Physiology, Nihon University School of Dentistry, Chiba, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 1999 Nov;124(3):327-32. doi: 10.1016/s0305-0491(99)00127-3.
Phosphofructokinase (EC 2.7.1.11) is a major enzyme of the glycolytic pathway, catalyzing the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate. In this study, we demonstrated the effect of ribose 1,5-bisphosphate on phosphofructokinase purified from rat kidney cortex. Ribose 1,5-bisphosphate relieved the phosphofructokinase from ATP inhibition and increased the affinity for fructose 6-phosphate at nanomolar concentrations. These activating effects of ribose 1,5-bisphosphate were enhanced in the presence of AMP. Ribose 1,5-bisphosphate reduced the inhibition of the phosphofructokinase induced by citrate. These results suggest that ribose 1,5-bisphosphate is an activator of rat kidney cortex phosphofructokinase and synergistically regulates the enzyme activity with AMP.
磷酸果糖激酶（EC 2.7.1.11）是糖酵解途径的一种主要酶，催化6-磷酸果糖转化为1,6-二磷酸果糖。在本研究中，我们展示了1,5-二磷酸核糖对从大鼠肾皮质纯化的磷酸果糖激酶的影响。1,5-二磷酸核糖可使磷酸果糖激酶免受ATP抑制，并在纳摩尔浓度下增加其对6-磷酸果糖的亲和力。在AMP存在的情况下，1,5-二磷酸核糖的这些激活作用会增强。1,5-二磷酸核糖可减轻柠檬酸对磷酸果糖激酶的抑制作用。这些结果表明，1,5-二磷酸核糖是大鼠肾皮质磷酸果糖激酶的激活剂，并与AMP协同调节该酶的活性。
