pfk 1

PFK1, also known as PFKM, is a regulatory glycolytic enzyme. PFK1 converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. It is a muscle-type isozyme. There are three phosphofructokinase isozymes in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Mutations in PFK1 gene have been related to glycogen storage disease type VII, also identified as Tarui disease.

Fructose-1,6-Bisphosphatase 1 (FBPase 1) is a member of the FBPase class 1 family. FBPase 1 is a gluconeogenesis regulatory protein, which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBPase 1 can assume an active R-state, or an inactive T-state. FBPase 1 deficiency is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis in newborn infants or young children. FBPase 1 coupled with phosphofructokinase (PFK) is involved in the metabolism of pancreatic islet cells.

6-phosphofructokinase, muscle type is a muscle-type isozyme that in humans is encoded by the PFKM gene. It belongs to the phosphofructokinase family and Two domains subfamily. PFKM functions as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. PFK1 converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP.

Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, is a potent activator of phosphofructokinase, which is a rate-limiting enzyme of glycolysis. Highly phosphorylated PFKFB3 protein was found in human tumor cells, vascular endothelial cells, and smooth muscle cells. Fructose 2,6-bisphosphate (Fru-2,6-BP) is an allosteric activator of 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in glycolysis. The concentration of PFK2 depends on the activity of the bifunctional enzyme, 6-phosphofructo-2-kinase fructose-2,6-bisphosphatase (PFK-2 FBPase). PFK2 controls the glycolytic flux via the allosteric activator fructose 2,6-bisphosphate. Because of its proto-oncogenic character, the PFK-2 FBPase-2 of the PFKFB3 gene is assumed to play a critical role in tumorigenesis. The hypoxia-inducible form of 6-phosphofructo-2-kinase fructose-2,6-bisphosphatase (PFKFB3) plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severely hypoxic conditions.

Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls the activity of the enzymes phosphofructokinase 1 (PFK-1) and fructose 1,6-bisphosphatase (FBPase-1) to regulate glycolysis and gluconeogenesis. Highly phosphorylated PFKFB3 protein was found in human tumor cells, vascular endothelial cells, and smooth muscle cells. Because of its proto-oncogenic character, the PFK-2 FBPase-2 of the PFKFB3 gene is assumed to play a critical role in tumorigenesis. PFKFB3 also plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions, which makes it a potential target for cancer therapy.