PK-RO

Pyruvate Kinase (PK)

from rabbit muscle

• Synonyme(s) : PK
• UNSPSC Code: 12352204
• Numéro CE : 2.7.1.40 (BRENDA, IUBMB)
• NACRES: NA.54
• Specific activity: ~200 units/mg protein (at 25 °C (500 U/mg at 37 °C) with PEP as the substrate.)
• Biological source: rabbit muscle

Propriétés

• biological source: rabbit muscle
• form: suspension
• specific activity: ~200 units/mg protein (at 25 °C (500 U/mg at 37 °C) with PEP as the substrate.)
• packaging: pkg of 1 mL (10128155001 [10 mg]), pkg of 10 mL (10128163001 [100 mg])
• manufacturer/tradename: Roche
• optimum pH: 7.0-7.5
• storage temp.: 2-8°C

Description

General description

ATP:pyruvate 2-O-phosphotransferase
Pyruvate kinase has a molar mass of 237,000 and exists as a tetramer. Each polypeptide chain of this tetramer has a molar mass of 57,200. The enzyme contains two identical catalytic particles called protomers. Each of these protomers contains two polypeptide chains. Each protomer contains one site each for Mn²⁺ and phosphoenolpyruvate.[1]

Application

Pyruvate kinase has been used to measure ATPase activity[2] and in the determination of adenylate concentration.[3]

Biochem/physiol Actions

Pyruvate kinase catalyzes the irreversible conversion of P-enolpyruvate and ADP to pyruvate and ATP with the utilization of a proton. The first step is the transfer of phosphate group from P-enolpyruvate to ADP with the formation of bound enolate of pyruvate and ATP. In the second step, a proton is added to enolate to generate the keto form of pyruvate. Apart from this, the enzyme exhibits other activities, such as ATP- and bicarbonate-dependent ATPase, phosphorylation of fluoride and hydroxylamine, ATP-dependent phosphorylation of glycolate, and decarboxylation of oxaloacetate.[4]

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Preparation Note

Activator: PK requires Mg²⁺ (or Mn²⁺, Co²⁺) and K⁺ (or NH⁴⁺, Rb⁺) for full activity.

Analysis Note

Contaminants: <0.001% GK, <0.002% “NADH oxidase”, and ATPase, each, <0.01% enolase, LDH, and myokinase, each

Other Notes

For life science research only. Not for use in diagnostic procedures.

Informations sur la sécurité

• Classe de stockage: 12 - Non Combustible Liquids
• wgk: WGK 1
• flash_point_f: No data available
• flash_point_c: No data available