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10109045001

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Synonyme(s) :

PK

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352204

Source biologique

rabbit muscle

Niveau de qualité

Forme

solution

Activité spécifique

~200 units/mg protein (At 25 °C with PEP as the substrate.)

Conditionnement

pkg of 1 mL (10 mg)

Fabricant/nom de marque

Roche

pH optimal

7.0-7.5

Conditions d'expédition

dry ice

Température de stockage

−20°C (−15°C to −25°C)

Catégories apparentées

Description générale

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.

Spécificité

Specific activity: Approximately 200 U/mg at +25°C with PEP as the substrate.

Application

Pyruvate Kinase (PK) has been used as a sample in ATPase Assays.
Pyruvate Kinase (PK) has been used in the kinase assay.

Actions biochimiques/physiologiques

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. The enzyme also exhibits other activities, such as ATP- and bicarbonate-dependent ATPase, phosphorylation of fluoride and hydroxylamine, ATP-dependent phosphorylation of glycolate, and decarboxylation of oxaloacetate.

Qualité

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

Forme physique

Solution in 50% glycerol (v/v), pH approximately 6

Notes préparatoires

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

Autres remarques

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

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

No data available

Point d'éclair (°C)

No data available


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

In vivo evidence for ATPase-dependent DNA translocation by the Bacillus subtilis SMC condensin complex
Wang X, et al.
Molecular Cell, 71(5), 841-847 (2018)
Ryo R Watanabe et al.
iScience, 26(5), 106626-106626 (2023-05-17)
F1-ATPase (F1) is an ATP-driven rotary motor protein ubiquitously found in many species as the catalytic portion of FoF1-ATP synthase. Despite the highly conserved amino acid sequence of the catalytic core subunits: α and β, F1 shows diversity in the
Matthias M Schneider et al.
Nature communications, 12(1), 5999-5999 (2021-10-16)
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo protein folding and preventing amyloid formation. Chaperones of the Hsp70 family can further disaggregate otherwise irreversible aggregate species such as α-synuclein fibrils, which accumulate in Parkinson's
Metabolic control and structure of glycolytic enzymes. 3. Dissociation and subunit structure of rabbit muscle pyruvate kinase.
M A Steinmetz et al.
Biochemistry, 5(4), 1399-1405 (1966-04-01)
The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
Rivera-Calzada A, et al.
Structure, 25(7), 1145-1152 (2017)

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