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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-633-5
MDL number:
Specific activity:
≥50 units/mg protein
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Laissez-nous vous aiderNom du produit
Fructose-6-phosphate Kinase from Bacillus stearothermophilus, Type VII, lyophilized powder, ≥50 units/mg protein
type
Type VII
form
lyophilized powder
specific activity
≥50 units/mg protein
mol wt
34 kDa
shipped in
wet ice
storage temp.
−20°C
Quality Level
Catégories apparentées
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).
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.
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.
Bacillus stearothermophilus phosphofructokinase (BsPFK) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (PEP), which binds along one dimer-dimer interface.
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.
Physical form
Lyophilized powder containing buffer salt (e.g. phosphate buffer, or Tris buffer with NaCl)
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Analysis of the phosphofructokinase subunits and isoenzymes in human tissues
G.A. Dunaway et al.
The Biochemical Journal, 251, 755-757 (1988)
M D Wallace et al.
Oncogene, 33(28), 3688-3695 (2013-08-27)
Defective DNA replication can result in genomic instability, cancer and developmental defects. To understand the roles of DNA damage response (DDR) genes on carcinogenesis in mutants defective for core DNA replication components, we utilized the Mcm4(Chaos3/Chaos3) ('Chaos3') mouse model that
Rockann Mosser et al.
Biochemistry, 52(32), 5421-5429 (2013-07-19)
Bacillus stearothermophilus phosphofructokinase (BsPFK) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (PEP), which binds along one dimer-dimer interface. The substrate, fructose 6-phosphate (Fru-6-P), binds along the other dimer-dimer interface. Evans et al. observed that the structure with inhibitor
Gamut of glycolytic enzymes in vascular smooth muscle cell proliferation: Implications for vascular proliferative diseases
Sarkar A, et al.
Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 167021-167021 (2024)
Loss of positive allosteric interactions between neuronal nitric oxide synthase and phosphofructokinase contributes to defects in glycolysis and increased fatigability in muscular dystrophy
Wehling-Henricks M, et al.
Human Molecular Genetics, 18(18), 3439-3451 (2009)
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