P7634
3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae)
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
Recommended Products
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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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.
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.
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Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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J P Doucet et al.
The Journal of biological chemistry, 266(26), 17613-17620 (1991-09-15)
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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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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