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MilliporeSigma

10109045001

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Sinónimos:

PK

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352204

biological source

rabbit muscle

Quality Level

form

solution

specific activity

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

packaging

pkg of 1 mL (10 mg)

manufacturer/tradename

Roche

optimum pH

7.0-7.5

shipped in

dry ice

storage temp.

−20°C (−15°C to −25°C)

Categorías relacionadas

General description

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.

Specificity

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.

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. 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.

Quality

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

Physical form

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

Preparation Note

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

Other Notes

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

No data available

flash_point_c

No data available


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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
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)
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)
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)
T M Larsen et al.
Biochemistry, 33(20), 6301-6309 (1994-05-24)
The molecular structure of rabbit muscle pyruvate kinase, crystallized as a complex with Mn2+, K+, and pyruvate, has been solved to 2.9-A resolution. Crystals employed in the investigation belonged to the space group P1 and had unit cell dimensions a

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