Pyruvate Kinase from rabbit muscle Type II, ammonium sulfate suspension, 350-600 units/mg protein

Properties

Related Categories	2.7.x.x Phosphorus containing groups, 2.x.x.x Transferases, Application Index, Biochemicals and Reagents, Diagnostic and Analytical Enzymes, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, General Metabolic Enzymes, General Metabolic Enzymes I-Z, Glycolysis, Glycolysis Enzymes, Metabolic Pathways, Metabolomics More...
type	Type II
form	ammonium sulfate suspension
foreign activity	lactic dehydrogenase, creatine phosphokinase, and myokinase ≤0.01%
	phosphoglucomutase ≤0.05%
storage temp.	2-8°C

Description

Analysis Note

Protein determined by biuret.

General description

Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate. ²

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 2.9 M (NH₄)₂SO₄ solution

Application

Pyruvate kinase from rabbit muscle has been used in a structural study to understand the reaction mechanism of the final step in glycolysis. ¹ It has also been used in a study to investigate ATP-dependent phosphorylation of α-substituted carboxylic acids. ²

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 K_M 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⁺).