Not available outside of the UK & Ireland.

Application

Fructose-6-phosphate kinase from Bacillus stearothermophilus has been used:in steady state analysis of phosphofructokinase activity in the presence of ATP deuterated at the C8 position(C8-D ATP)for standard curve generation for quantifying muscle phosphofructokinase (PFK) activity

Fructose-6-phosphate Kinase from Bacillus stearothermophilus was shown to interact with neuronal nitric oxide synthase (nNOS) causing a defect in glycolytic metabolism and increased fatigability in dystrophic muscle.

Biochem/physiol Actions

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.

General description

Fructose-6-phosphate kinase from Bacillus stearothermophilus, a 34 kDa enzyme, belongs to phosphofructokinase (PFK) - like superfamily. The glutamate 161 and arginine 162 residues at the active site are crucial for substrate binding.

Bacillus stearothermophilus phosphofructokinase (BsPFK) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (PEP), which binds along one dimer-dimer interface.

Packaging

100, 250 units in glass bottle

Physical form

Lyophilized powder containing buffer salt (e.g. phosphate buffer, or Tris buffer with NaCl)

Unit Definition

One unit will convert 1.0 µmole of fructose 6-phosphate and ATP to fructose 1,6-diphosphate and ADP per minute at pH 9.0 at 30 °C.