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Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ...
PFK belongs to the phosphofructokinase B (PfkB) family of sugar kinases. [7] Other members of this family (also known as the Ribokinase family) include ribokinase (RK), adenosine kinase (AK), inosine kinase, and 1-phosphofructokinase. [7] [8] [9] The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs.
Phosphofructokinase deficiency is a rare muscular metabolic disorder, with an autosomal recessive inheritance pattern. It is characterized as a deficiency in the Phosphofructokinase (PFK) enzyme throughout the body, including the skeletal muscles and red blood cells.
Fructose 2,6-bisphosphate, abbreviated Fru-2,6-P 2, is a metabolite that allosterically affects the activity of the enzymes phosphofructokinase 1 (PFK-1) and fructose 1,6-bisphosphatase (FBPase-1) to regulate glycolysis and gluconeogenesis.
Phosphofructokinase (generally referred to as PFK) is an enzyme that catalyses the third step of glycolysis: the phosphorylation of fructose-6-phosphate into fructose 1,6-bisphosphate. PFK can be allosterically inhibited by high levels of ATP within the cell.
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