P7634

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

Name: 3-Phosphoglyceric Phosphokinase from baker′s yeast (<I>S. cerevisiae</I>)
Brand: SIGMA

ammonium sulfate suspension, ≥500 units/mg protein

Synonym(s):

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

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About This Item

CAS Number:

9001-83-6

UNSPSC Code:

12352204

eCl@ss:

32160410

EC Number:

232-636-1

NACRES:

NA.54

MDL number:

MFCD00130301

EC Number:

2.7.2.3 (BRENDA, IUBMB)

Product Name

3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae), ammonium sulfate suspension, ≥500 units/mg protein

biological source

bakers yeast

form

ammonium sulfate suspension

specific activity

≥500 units/mg protein

storage condition

(Tightly closed)

concentration

1.0-10.0 mg/mL

foreign activity

Glyceraldehyde-3-phosphate dehydrogenase ≤0.1%

shipped in

wet ice

storage temp.

2-8°C

Quality Level

200

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Analysis Note

Protein determined by TCA Biuret.

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

Biochem/physiol Actions

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.

General description

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.

Other Notes

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

Physical form

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

pictograms

GHS07

signalword

Warning

hcodes

H319

pcodes

P264 - P280 - P305 + P351 + P338 - P337 + P313

Hazard Classifications

Eye Irrit. 2

Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Enzyme activity in the crowded milieu.

Tobias Vöpel et al.

PloS one, 7(6), e39418-e39418 (2012-07-05)

The cytosol of a cell is a concentrated milieu of a variety of different molecules, including small molecules (salts and metabolites) and macromolecules such as nucleic acids, polysaccharides, proteins and large macromolecular complexes. Macromolecular crowding in the cytosolic environment is

Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.

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

Identification of the actin and plasminogen binding regions of group B streptococcal phosphoglycerate kinase.

Tyler J Boone et al.

The Journal of biological chemistry, 287(34), 29035-29044 (2012-07-05)

Phosphoglycerate kinase (PGK), present on the surface of group B streptococcus (GBS), has previously been demonstrated to bind the host proteins actin and plasminogen. The actin and plasminogen binding sites of GBS-PGK were identified using truncated GBS-PGK molecules, followed by

Epigenetic deregulation of miR-29a and miR-1256 by isoflavone contributes to the inhibition of prostate cancer cell growth and invasion.

Yiwei Li et al.

Epigenetics, 7(8), 940-949 (2012-07-19)

The epigenetic regulation of genes has long been recognized as one of the causes of prostate cancer (PCa) development and progression. Recent studies have shown that a number of microRNAs (miRNAs) are also epigenetically regulated in different types of cancers

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea

Pirela MR, et al.

Open Biology (2020)

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