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F0137

Sigma-Aldrich

Fructose-6-phosphate Kinase from Bacillus stearothermophilus

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

Synonym(s):

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

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About This Item

CAS Number:
9001-80-3
Enzyme Commission number:
2.7.1.11 (BRENDA, IUBMB)
EC Number:
232-633-5
MDL number:
MFCD00131107
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type VII

Quality Level

200

form

lyophilized powder

specific activity

≥50 units/mg protein

mol wt

34 kDa

shipped in

wet ice

storage temp.

−20°C

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.

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).

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.

Physical form

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

F0137-50UN:
F0137-VAR:
F0137-250UN:
F0137-100UN:
F0137-BULK:

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Certificates of Analysis (COA)

Lot/Batch Number
0000363401
0000363401
0000317272
0000334023
0000264148

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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)
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)
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
The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases
Kenyon CP, et al.
BMC Biochemistry, 12(1), 36-36 (2011)
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