Description
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[3]). This protein may use the morpheein model of allosteric regulation.
Abbr
PFK, Native (Bacillus stearothermophilus)
Source
Bacillus stearothermophilus
Applications
Useful for enzymatic determiantion of fructose-6-phosphate
Appearance
White to pale yellow powder
Product Overview
Is an enzyme produced by microorganisms. This product shall be used for a diagnostics reagent.
Enzyme Commission Number
EC 2.7.1.11
Contaminants
NADPH oxidase < 0.01%; ATPase < 0.005%
Molecular Weight
72 kDa (gel filtration); 35 kDa (SDS‒PAGE)
pH Stability
6.0-10.0 (37°C, 60 mins)
Michaelis Constant
D‒Fructose‒6‒phosphate (D‒F‒6‒P) 5.8 mM (at 37°C); ATP 0.07 mM (at 37°C)
Unit Definition
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.
Thermal stability
Stable at 55°C and below (pH 8.5, 30 mins)
Storage
Storage at-20°C in the presence of a desiccant is recommended.
Synonyms
PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase
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