Sigma-Aldrich 3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae). ammonium sulfate suspension, ≥500 units/mg protein. 2000 units

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.[1]

3-Phosphoglyceric Phosphokinase from baker′s yeast (S. cerevisiae) has been used:

• to study low molecular weight GTP-binding proteins[2] and mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase[3]
• in the coupled assay to measure the backward activity of purified rabbit skeletal muscle nicotinamide adenine dinucleotide (NAD⁺)-dependent glyceraldehyde3-phosphate dehydrogenase (GAPDH)[4]
• in the assay of glyceraldehyde-3-phosphate dehydrogenase[5]

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.[1]

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

Protein determined by TCA Biuret.

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