P7634
3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae)
ammonium sulfate suspension, ≥500 units/mg protein
Sinónimos:
PGK, Phosphoglycerate kinase, 3-Phosphoglycerate kinase, ATP:3-Phospho-D-glycerate 1-phosphotransferase
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About This Item
Número CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-636-1
NACRES:
NA.54
MDL number:
Nombre del producto
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
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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.
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
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2
Clase de almacenamiento
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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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
Tobias Vöpel et al.
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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
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