Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation.
PFK, Native (Bacillus stearothermophilus)
Useful for enzymatic determiantion of fructose-6-phosphate
White to pale yellow powder
Is an enzyme produced by microorganisms. This product shall be used for a diagnostics reagent.
Enzyme Commission Number
NADPH oxidase < 0.01%; ATPase < 0.005%
72 kDa (gel filtration); 35 kDa (SDS‒PAGE)
6.0-10.0 (37°C, 60 mins)
D‒Fructose‒6‒phosphate (D‒F‒6‒P) 5.8 mM (at 37°C); ATP 0.07 mM (at 37°C)
One unit is defined as the amount of enzyme which converts 1 μmole of fructose‒6‒phosphate to Fructose‒1,6 ‒bisphosphate per minute at 37°C under the conditions specified in the assay procedure.
Stable at 55°C and below (pH 8.5, 30 mins)
Storage at-20°C in the presence of a desiccant is recommended.
PFKWII; EC 220.127.116.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase