Recombinant Human PFKFB1 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PFKFB1 also known as 6-phosphofructo-2-kinase/fructose-26-bisphosphatase 1 plays an important role in glycolysis and gluconeogenesis. It catalyzes the synthesis and degradation of fructose-26-bisphosphate (F26BP) a potent regulator of the glycolytic flux. This protein has an approximate mass of 58-60 kDa and shows expression predominantly in liver and adipose tissue. Its distinct structure allows it to switch between kinase and phosphatase activities.

Biological function summary

PFKFB1 modulates the balance of carbohydrate metabolism. The protein manages levels of F26BP facilitating enhanced glycolysis or gluconeogenesis depending on metabolic demands. PFKFB1 does not form part of a larger enzymatic complex but it operates by itself to regulate metabolic processes. Its regulation involves allosteric changes and phosphorylation by other enzymes reflecting its importance in maintaining energy homeostasis.

Pathways

PFKFB1 features in both glycolytic and gluconeogenic pathways. The glycolysis pathway sees PFKFB1 influencing how cells convert glucose into pyruvate generating ATP. In the gluconeogenesis pathway PFKFB1 also contributes to converting non-carbohydrates into glucose. It interacts with proteins such as phosphofructokinase-1 (PFK-1) and fructose-16-bisphosphatase (FBPase-1) key regulators of the metabolic flux alongside PFKFB1.

Metabolic dysregulation involving PFKFB1 could relate to conditions like diabetes and metabolic syndrome. Abnormal PFKFB1 activity might affect glycolytic and gluconeogenic balance impacting glucose levels and energy management. It connects to insulin influencing insulin resistance and subsequent glucose uptake. Other proteins such as AKT and AMP-activated protein kinase (AMPK) interact with PFKFB1 during these conditions affecting its regulatory capacity on metabolism.