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Merck

F0137

Fructose-6-phosphate Kinase from Bacillus stearothermophilus

Type VII, lyophilized powder, ≥50 units/mg protein

Synonyme(s) :

6-Phosphofructokinase, ATP:D-fructose 6-phosphate 1-phosphotransferase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-633-5
MDL number:
Numéro CE :
Specific activity:
≥50 units/mg protein
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Nom 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.

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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Consulter la Bibliothèque de documents

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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