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P7634

Sigma-Aldrich

3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae)

ammonium sulfate suspension, ≥500 units/mg protein

Synonyme(s) :

PGK, Phosphoglycerate kinase, 3-Phosphoglycerate kinase, ATP:3-Phospho-D-glycerate 1-phosphotransferase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

bakers yeast

Forme

ammonium sulfate suspension

Activité spécifique

≥500 units/mg protein

Conditions de stockage

(Tightly closed)

Concentration

1.0-10.0 mg/mL

Activité étrangère

Glyceraldehyde-3-phosphate dehydrogenase ≤0.1%

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Description générale

Research area: Cell Signaling

Phosphoglycerate kinase (PGK), a glycolytic enzyme, is isolated from a broad variety of organisms. This typical hinge-bending monomeric enzyme is well-conserved among the three domains of life. The enzyme is made up of a single folded polypeptide chain that divides into two nearly identical domains, each linked by two -helices (-helices 7 and 14) and separated by a deep cleft. This arrangement gives the enzyme its distinctive bilobed structure.

Application

3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae) has been used:
  • to study low molecular weight GTP-binding proteins and mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase
  • in the coupled assay to measure the backward activity of purified rabbit skeletal muscle nicotinamide adenine dinucleotide (NAD+)-dependent glyceraldehyde3-phosphate dehydrogenase (GAPDH)
  • in the assay of glyceraldehyde-3-phosphate dehydrogenase

Actions biochimiques/physiologiques

3-Phosphoglyceric phosphokinase catalyzes the reversible transfer of a phosphate group from 1,3-diphosphoglycerate to ADP to generate ATP and 3-phosphoglycerate. 3-Phosphoglycerate phosphokinase activity is essential for glycolysis and gluconeogenesis. Phosphoglyceratekinase (PGK) plays a vital role in the glycolytic pathway by catalyzing one of the two ATP-producing reactions. It converts 1,3-bisphosphoglycerate (1,3BPGA) to 3-phosphoglycerate (3PGA). Additionally, it takes part in the process of gluconeogenesis by catalyzing the opposite reaction to create 1,3BPGA and adenosine diphosphate (ADP). Due to its participation in numerous processes other than energy metabolisms, such as pathogenesis, interaction with nucleic acids, tumorigenesis progression, cell death, and viral replication, PGK is also known as a moonlighting protein.

Définition de l'unité

One unit will convert 1.0 μmole of 1,3-diphosphoglycerate to 3-phosphoglycerate per min at pH 6.9 at 25 °C.

Forme physique

Crystalline suspension in 3.0 M (NH4)2SO4 and 0.04 M tetrasodium pyrophosphate solution, pH 8.0

Remarque sur l'analyse

Protein determined by TCA Biuret.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Angelika B Riemer et al.
Experimental dermatology, 21(8), 625-629 (2012-07-11)
Based on the exquisite sensitivity, reproducibility and wide dynamic range of quantitative reverse-transcription real-time polymerase chain reaction (qRT-PCR), it is currently the gold standard for gene expression studies. Target gene expression is calculated relative to a stably expressed reference gene.
Paule Bénit et al.
EBioMedicine, 17, 75-87 (2017-02-24)
Mice with the hypomorphic AIF-Harlequin mutation exhibit a highly heterogeneous mitochondriopathy that mostly affects respiratory chain complex I, causing a cerebral pathology that resembles that found in patients with AIF loss-of-function mutations. Here we describe that the antidiabetic drug pioglitazone
Kayla Baretta et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 7), 790-792 (2012-07-04)
Acinetobacter baumannii is a common multidrug-resistant clinical pathogen that is often found in hospitals. The A. baumannii phosphoglycerate kinase (AbPGK) is involved in the key energy-producing pathway of glycolysis and presents a potential target for antibiotic development. AbPGK has been
Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea
Pirela MR, et al.
Open Biology (2020)
Gergely Agócs et al.
Biophysical journal, 102(12), 2828-2834 (2012-06-28)
Partitioning of polypeptides between protein folding and amyloid formation is of outstanding pathophysiological importance. Using yeast phosphoglycerate kinase as model, here we identify the features of the energy landscape that decide the fate of the protein: folding or amyloidogenesis. Structure

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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