STRUCTURAL AND FUNCTIONAL STUDIES OF EUKARYOTIC PHOSPHOFRUCTOKINASE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 磷酸果糖激酶(Pfk1)催化糖酵解的关键调节步骤，即在三磷酸腺苷存在下将果糖6-磷酸(F6P)磷酸化为果糖1，6-二磷酸。Pfk1的酶活性受多种变构效应调控，表明该酶在糖酵解通量的调节中起着关键作用。糖酵解是癌细胞的主要能量来源。因此，彻底了解Pfk1的结构/功能关系可能会导致对某些类型的癌症进行新的、更有效的治疗。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Phosphofructokinase (Pfk1) catalyzes a crucial regulatory step of glycolysis, the phosphorylation of fructose 6-phosphate (F6P) to fructose 1,6-biphosphate in the presence of ATP. The enzymatic activity of Pfk1 is controlled by many allosteric effectors, evidencing the key role that the enzyme plays in the regulation of the glycolytic flux. Glycolysis is the main energy source of cancer cells. Thus, a thorough understanding of the structure/function relationship in Pfk1 may lead to novel and more effective treatments for certain types of cancer.