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Key Documents

P1506

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type II, ammonium sulfate suspension, 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 MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

rabbit muscle

Niveau de qualité

Type

Type II

Forme

ammonium sulfate suspension

Activité spécifique

350-600 units/mg protein

Poids mol.

237 kDa

Conditions de stockage

(Tightly closed)

Technique(s)

ligand binding assay: suitable

Couleur

white

Activité étrangère

lactic dehydrogenase, creatine phosphokinase, and myokinase ≤0.01%
phosphoglucomutase ≤0.05%

Température de stockage

2-8°C

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Description générale

Research Area: Cell Signaling

Pyruvate kinase from rabbit muscle catalyzes ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate.Pyruvate kinase, an enzyme, is found in a tetrameric or a dimeric form. PKM1, PKM2, PKR, and PKL are the four mammalian pyruvate kinase isoforms.

Application

Pyruvate kinase from rabbit muscle has been used in:

  • a structural study to understand the reaction mechanism of the final step in glycolysis.
  • a study to investigate ATP-dependent phosphorylation of α-substituted carboxylic acids.
  • enzyme assays.

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 from rabbit muscle can be activated by histidine and inhibited by low levels of zinc (Zn2+). In the glycolytic pathway, pyruvate kinase (PK) functions as a terminal enzyme, catalyzing the conversion of phosphoenolpyruvate to pyruvate and the synthesis of ATP through substrate-level phosphorylation. Tetrameric structures of PK are more active and have a high affinity for phosphoenolpyruvate (PEP), whereas dimeric structures are less active and have a low affinity for PEP. PK from rabbit muscle possesses positive kinetic cooperativity (Hill coefficient> 1.35) of the phosphoenol pyruvate and adenosine diphosphate(ADP) binding sites.

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.

Forme physique

Suspension in 3.2 M (NH4)2SO4 solution, pH 6

Remarque sur l'analyse

Protein determined by biuret.

Substrat

Réf. du produit
Description
Tarif

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

D E Ash et al.
Archives of biochemistry and biophysics, 228(1), 31-40 (1984-01-01)
Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate (F. J. Kayne (1974) Biochem. Biophys. Res. Commun. 59, 8-13). An investigation of anologous reactions with other alpha-substituted carboxylic acids reveals several new substrates for such
Xun Chen et al.
Cancer cell international, 20(1), 523-523 (2020-12-10)
Pyruvate kinase is a terminal enzyme in the glycolytic pathway, where it catalyzes the conversion of phosphoenolpyruvate to pyruvate and production of ATP via substrate level phosphorylation. PKM2 is one of four isoforms of pyruvate kinase and is widely expressed
Glucokinase in Atlantic Halibut (Hippoglossus hippoglossus) Brockmann Bodies
Tranulis MA, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 116, 367-370 (1997)
Inhibitory effect of Zn2+ on rabbit muscle pyruvate kinase and reactivation by histidine.
Tamaki N.
J. Nutr. Sci. Vitaminol., 27, 107-116 (1981)
S Strumilo et al.
Zhurnal evoliutsionnoi biokhimii i fiziologii, 51(2), 103-107 (2015-06-02)
Some catalytic and kinetic properties of pyruvate kinase (PK, EC 2.7.1.40) isolated from the heart and skeletal muscles of rabbits and hares with a 9-16-fold purification were studied. The initial specific activity of the enzyme in hare heart homogenates was

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