F8381
Fructose-6-phosphate Kinase, Pyrophosphate-dependent from Propionibacterium freudenreichii (shermanii)
lyophilized powder, ≥4.0 units/mg protein
Synonym(s):
6-Phosphofructokinase(pyrophosphate), Pyrophosphate: D-fructose-6-phosphate 1-phosphotransferase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
form
lyophilized powder
Quality Level
specific activity
≥4.0 units/mg protein
composition
Protein, 5.0-25.0% biuret
storage temp.
−20°C
Application
FBP was used to study the kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.
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.
Other Notes
These two pyrophosphate-dependent fructose-6-phosphate kinases differ in their response to the physiological activator fructose 2,6-diphosphate [Fru (2,6)-P2]. The enzyme from Propionibacterium freudenreichii (F8381) reportedly is not affected by Fru (2,6)-P2. The enzyme from potato tubers (F2258) is stimulated by Fru (2,6)-P2 (half-maximal activation at 5.5 nM Fru (2,6)-P2 for potato tuber enzyme).
Unit Definition
One unit will convert 1.0 μmole of pyrophosphate and fructose 6-phosphate to fructose 1,6-diphosphate and inorganic phosphate per min at pH 7.4 at 30 °C.
Physical form
Contains imidazole salts and stabilizer
signalword
Danger
hcodes
Hazard Classifications
Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Corr. 1C
Storage Class
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificates of Analysis (COA)
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Corrigendum: Online Pyrophosphate Assay for Analyzing Adenylation Domains of Nonribosomal Peptide Synthetases.
Tiia Kittilä et al.
Chembiochem : a European journal of chemical biology, 23(18), e202200381-e202200381 (2022-07-28)
Daniel L Machell et al.
Chembiochem : a European journal of chemical biology, 23(18), e202200325-e202200325 (2022-07-26)
Detection of pyrophosphate is important in quantifying enzyme activity, particularly adenylation domain activity during non-ribosomal peptide synthesis. The previous development of an enzyme coupled PPi /NADH assay allowed the measurement of such activity in an online fashion using commercially available
B L Bertagnolli et al.
Biochemistry, 23(18), 4101-4108 (1984-08-28)
Inorganic pyrophosphate dependent D-fructose-6-phosphate 1-phosphotransferase from Propionibacterium freudenreichii was purified to apparent homogeneity by the criterion of silver staining on sodium dodecyl sulfate (SDS) gels. In the direction of phosphorylation of fructose 6-phosphate (F6P), an intersecting initial velocity pattern is
T H Nielsen et al.
Planta, 214(1), 106-116 (2002-01-05)
The role of pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) in developing leaves was studied using wild-type tobacco (Nicotiana tabacum L.) and transformants with decreased expression of PFP. (i) The leaf base, which is the youngest and most actively growing area of the leaf
Florencio E Podestá et al.
Archives of biochemistry and biophysics, 414(1), 101-107 (2003-05-15)
The intrinsic fluorescence of potato tuber pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) was used as an indicator of conformational changes due to ligand binding. Binding of the substrates and the allosteric activator fructose-2,6-bisphosphate was quantitatively compared to their respective kinetic effects on enzymatic
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