Fructose-6-phosphate Kinase from Bacillus stearothermophilus

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

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.

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.

Fructose-6-phosphate Kinase from Bacillus stearothermophilus has been used in the assay mixture for mass spectrometry assay for phosphoglucoisomerase (PGI) (G6P to F6P reaction).

Phosphofructokinase (PFK) is an essential bifunctional enzyme that serves as a critical regulator in the intermediate stages of glycolysis. PFK is strongly linked to caveolae and is brought to caveolae by caveolin-1 in vascular smooth muscle cells (VSMCs).

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.

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

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.