P1506
Pyruvate Kinase from rabbit muscle
Type II, ammonium sulfate suspension, 350-600 units/mg protein
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Synonym(s):
ATP:pyruvate 2-O-phosphotransferase, PK
CAS Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Recommended Products
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.
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.
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.
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enzyme
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related product
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substrate
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WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
动植物源性产品
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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
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)
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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