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P7634

Sigma-Aldrich

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

ammonium sulfate suspension, ≥500 units/mg protein

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Synonym(s):
PGK, Phosphoglycerate kinase, 3-Phosphoglycerate kinase, ATP:3-Phospho-D-glycerate 1-phosphotransferase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
32160410

biological source

bakers yeast

Quality Level

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

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This Item
U8501P5381G7877
specific activity

≥500 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥400 units/mg protein (biuret)

specific activity

≥200 units/mg protein

form

ammonium sulfate suspension

form

lyophilized powder

form

ammonium sulfate suspension

form

ammonium sulfate suspension

concentration

1.0-10.0 mg/mL

concentration

-

concentration

≥3 mg/mL protein Biuret

concentration

-

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

storage condition

(Tightly closed)

storage condition

-

storage condition

-

storage condition

-

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.

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.

Unit Definition

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

Analysis Note

Protein determined by TCA Biuret.

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Eye Irrit. 2

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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
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
R A Wolosiuk et al.
The Journal of biological chemistry, 251(20), 6456-6461 (1976-10-25)
Chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase was resolved into three forms that differed in molecular weight: (a) larger than or equal to 1.5 million; (b) 600,000; and (c) less than or equal to 100,000. After preincubation with an effector (ATP, NADPH, or
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

Articles

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