Orosz F, Christova T Y, Ovádi J
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest.
Biochem Biophys Res Commun. 1987 Sep 30;147(3):1121-8. doi: 10.1016/s0006-291x(87)80186-9.
The effect of aldolase on the concentration-dependent kinetic behaviour of phosphofructokinase was investigated by means of covalently attached fluorescent probe and by using a kinetic approach. The dimeric form of kinase in equilibrium with the active tetramer interacts with the native aldolase with an apparent dissociation constant of 2.5 microM. Within this heterologous enzyme complex the phosphofructokinase is catalytically active probably because the aldolase binding to nascent kinase dimers might protect them against inactivation.
通过共价连接的荧光探针并采用动力学方法，研究了醛缩酶对磷酸果糖激酶浓度依赖性动力学行为的影响。处于与活性四聚体平衡状态的激酶二聚体与天然醛缩酶相互作用，其表观解离常数为2.5微摩尔。在这种异源酶复合物中，磷酸果糖激酶具有催化活性，可能是因为醛缩酶与新生激酶二聚体的结合可能保护它们不被失活。
