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10109045001

Roche

Pyruvate Kinase (PK)

from rabbit muscle

Sinônimo(s):

PK

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About This Item

Número da licença da enzima:
Código UNSPSC:
12352204
Preço e disponibilidade não estão disponíveis no momento.

fonte biológica

rabbit muscle

Nível de qualidade

Formulário

solution

atividade específica

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

embalagem

pkg of 1 mL (10 mg)

fabricante/nome comercial

Roche

pH ideal

7.0-7.5

Condições de expedição

dry ice

temperatura de armazenamento

−20°C (−15°C to −25°C)

Categorias relacionadas

Descrição geral

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]

Especificidade

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

Aplicação

Pyruvate Kinase (PK) has been used as a sample in ATPase Assays.[2][3]
Pyruvate Kinase (PK) has been used in the kinase assay.[4]

Ações bioquímicas/fisiológicas

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.[5]

Qualidade

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

forma física

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

Nota de preparo

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

Outras notas

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

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

No data available

Ponto de fulgor (°C)

No data available


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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)
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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