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Wichtige Dokumente
F8381
Fructose-6-phosphate Kinase, Pyrophosphate-dependent from Propionibacterium freudenreichii (shermanii)
lyophilized powder, ≥4.0 units/mg protein
Synonym(e):
6-Phosphofructokinase(pyrophosphate), Pyrophosphate: D-fructose-6-phosphate 1-phosphotransferase
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
≥4.0 units/mg protein
Zusammensetzung
Protein, 5.0-25.0% biuret
Lagertemp.
−20°C
Anwendung
FBP was used to study the kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.[1]
Biochem./physiol. Wirkung
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.[2] Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle.[3][4]
Sonstige Hinweise
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).
Einheitendefinition
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.
Physikalische Form
Contains imidazole salts and stabilizer
Signalwort
Danger
H-Sätze
Gefahreneinstufungen
Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Corr. 1C
Lagerklassenschlüssel
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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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
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)
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
M Müller et al.
Journal of bacteriology, 183(22), 6714-6716 (2001-10-24)
Inorganic pyrophosphate-dependent phosphofructokinase (PP(i)-PFK) of the amitochondriate eukaryote Mastigamoeba balamuthi was sequenced and showed about 60% identity to PP(i)-PFKs from two eubacteria, Propionibacterium freudenreichii and Sinorhizobium meliloti. These gene products represent a newly recognized lineage of PFKs. All four lineages
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