Description
General description
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.
Application
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).
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
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.
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).
Physical form
Lyophilized powder containing buffer salt (e.g. phosphate buffer, or Tris buffer with NaCl)
Other Notes
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.
