STRUCTURAL AND FUNCTIONAL STUDIES OF EUKARYOTIC PHOSPHOFRUCTOKINASE

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 磷酸果糖激酶（Pfk 1）催化糖酵解的关键调节步骤，即在ATP存在下果糖6-磷酸（F6 P）磷酸化为果糖1，6-二磷酸。Pfk 1的酶活性受许多变构效应物控制，证明该酶在糖酵解通量调节中起关键作用。糖酵解是癌细胞的主要能量来源。因此，对Pfk 1结构/功能关系的深入了解可能会为某些类型的癌症带来新的更有效的治疗方法。

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.