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). This protein may use the morpheein model of allosteric regulation.
Abbr
PFK, Native (Thermophillic bacteria)
Source
Thermophillic bacteria
Applications
Diagnostic tests
Enzyme Commission Number
EC 2.7.1.11
Unit Definition
One unit is defined as the amount of enzyme oxidizing 1 µmol of NADH (ε340=6.22 mM-1 cm-1) per 1 minute using fructose 6-phosphate as a substrate.
Thermal stability
100% stability after 1 hour at 80°C
Buffer
20 mM Tris-HCl (pH 7.5), 20 mM KCl
Synonyms
PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase
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