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P9136

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type III, lyophilized powder, 350-600 units/mg protein

Synonyme(s) :

ATP:pyruvate 2-O-phosphotransferase, PK

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

rabbit muscle

Type

Type III

Forme

lyophilized powder

Activité spécifique

350-600 units/mg protein

Poids mol.

237 kDa

Activité étrangère

lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%

Température de stockage

−20°C

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Description générale

Pyruvate Kinase (PK) is a glycolysis enzyme and has four isozymes L, R, M1, and M2. The L isozyme is localized in gluconeogenic tissues, particularly in the liver. Whereas the R and M1 are localized in the adult skeletal muscles, heart, brain and erythrocytes, respectively. M2 is localized in the nucleus of the cells.

Application

Pyruvate Kinase from rabbit muscle has been used to convert adenosine diphosphate (ADP) to adenosine triphosphate (ATP) in Pseudomonas putida cells.
Pyruvate kinase has been used in plant spectrophotometric assays to measure ATP hydrolysis . Pyruvate kinase is also used to study pyruvate kinase (PK) deficiency .

Actions biochimiques/physiologiques

Molecular Weight: 237 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa.
Isoelectric Point: 7.6
Optimal pH: ∼7.5
Optimal Temperature: 25°C
ΕA280 = 0.54 for 1 mg(p)/ml, 1 cm path
Reported KM values are ATP (0.86 mM), pyruvate (10 mM), ADP (0.3 mM), and PEP (0.07 mM) in Tris buffer at pH 7.4 and 30 °C. Pyruvate kinase is highly specific for phosphoenolpyruvate, but can utilize other dinucleotide triphosphates as substrates in place of ATP including GTP, ITP, dATP, UTP, and CTP.
Pyruvate kinase (PK) catalyzes an important process of transferring phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP). This reaction results in the conversion of PEP to pyruvate and adenosine triphosphate (ATP). Pyruvate kinase plays a major role in glycolysis and gluconeogenesis. High levels of pyruvate kinase M2 (PKM2) inhibits cell proliferation and tumor growth. Deficiency of PK in red blood cells (RBC) leads to non-spherocytic hemolytic anaemia. In human erythrocytes, deficiency of PK induces a protective effect against Plasmodium falciparum.

Définition de l'unité

One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C.

Remarque sur l'analyse

Protein determined by biuret.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Pyruvate kinase deficiency and malaria
Ayi K, et al.
The New England Journal of Medicine, 358(17), 1805-1810 (2008)
Anoxic metabolism and biochemical production in Pseudomonas putida F1 driven by a bioelectrochemical system
Lai B, et al.
Biotechnology for Biofuels, 9(1), 39-39 (2016)
[25] Pyruvate kinase isozymes from rat
Methods in Enzymology, 90, 150-165 (1982)
Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis
Anastasiou D, et al.
Nature Chemical Biology, 8(10), 839-839 (2012)
S P Robinson et al.
Plant physiology, 88(4), 1008-1014 (1988-12-01)
Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) activase protein was purified from spinach leaves by ammonium sulfate precipitation and ion exchange fast protein liquid chromatography. This resulted in 48-fold purification with 70% recovery of activity and yielded up to 18 milligrams of rubisco

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