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P1506

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type II, ammonium sulfate suspension, 350-600 units/mg protein

Sinônimo(s):

ATP:pyruvate 2-O-phosphotransferase, PK

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About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

fonte biológica

rabbit muscle

tipo

Type II

forma

ammonium sulfate suspension

atividade específica

350-600 units/mg protein

peso molecular

237 kDa

condição de armazenamento

(Tightly closed)

técnica(s)

ligand binding assay: suitable

cor

white

atividade externa

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

temperatura de armazenamento

2-8°C

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Descrição geral

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.

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

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

forma física

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

Nota de análise

Protein determined by biuret.

substrato

Nº do produto
Descrição
Preços

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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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
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
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
Inhibitory effect of Zn2+ on rabbit muscle pyruvate kinase and reactivation by histidine.
Tamaki N.
J. Nutr. Sci. Vitaminol., 27, 107-116 (1981)
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)

Artigos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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