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P7634

Sigma-Aldrich

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

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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

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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.

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

Signal Word

Warning

Hazard 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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Angelika B Riemer et al.
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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
Paule Bénit et al.
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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
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Pirela MR, et al.
Open Biology (2020)
Katarzyna A Broniowska et al.
American journal of physiology. Heart and circulatory physiology, 299(4), H1212-H1219 (2010-08-03)
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Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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