STRUCTURAL AND FUNCTIONAL STUDIES OF EUKARYOTIC PHOSPHOFRUCTOKINASE

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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.