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P1506

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

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

Synonym(s):

ATP:pyruvate 2-O-phosphotransferase, PK

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

type

Type II

form

ammonium sulfate suspension

specific activity

350-600 units/mg protein

mol wt

237 kDa

storage condition

(Tightly closed)

technique(s)

ligand binding assay: suitable

color

white

foreign activity

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

storage temp.

2-8°C

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General description

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.

Biochem/physiol Actions

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.

Unit Definition

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

Physical form

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

Analysis Note

Protein determined by biuret.

Substrate

Product No.
Description
Pricing

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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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
Inhibitory effect of Zn2+ on rabbit muscle pyruvate kinase and reactivation by histidine.
Tamaki N.
J. Nutr. Sci. Vitaminol., 27, 107-116 (1981)
William J Israelsen et al.
Seminars in cell & developmental biology, 43, 43-51 (2015-08-19)
Pyruvate kinase is an enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP in glycolysis and plays a role in regulating cell metabolism. There are four mammalian pyruvate kinase isoforms with unique tissue expression patterns and
T M Larsen et al.
Biochemistry, 37(18), 6247-6255 (1998-06-13)
Pyruvate kinase from rabbit muscle has been cocrystallized as a complex with MgIIATP, oxalate, Mg2+, and either K+ or Na+. Crystals with either Na+ or K+ belong to the space group P2(1)2(1)2(1), and the asymmetric units contain two tetramers. The

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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