Fructose-6-phosphate Kinase, Pyrophosphate-dependent from Propionibacterium freudenreichii (shermanii)

FBP was used to study the kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.

Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle.

Contains imidazole salts and stabilizer

One unit will convert 1.0 μmole of pyrophosphate and fructose 6-phosphate to fructose 1,6-diphosphate and inorganic phosphate per min at pH 7.4 at 30 °C.

These two pyrophosphate-dependent fructose-6-phosphate kinases differ in their response to the physiological activator fructose 2,6-diphosphate [Fru (2,6)-P₂]. The enzyme from Propionibacterium freudenreichii (F8381) reportedly is not affected by Fru (2,6)-P₂. The enzyme from potato tubers (F2258) is stimulated by Fru (2,6)-P₂ (half-maximal activation at 5.5 nM Fru (2,6)-P₂ for potato tuber enzyme).