Recombinant Cricetulus griseus Phosphoglycerate kinase 1 (PGK1)

Function

Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). Acts as a protein kinase when localized to the mitochondrion where it phosphorylates pyruvate dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex activity and suppress the formation of acetyl-coenzyme A from pyruvate, and consequently inhibit oxidative phosphorylation and promote glycolysis. May play a role in sperm motility

Subcellular Location

Cytoplasm, cytosol; Mitochondrion matrix

Subunit

Monomer. Interacts with kinase MAPK1/ERK2; the interaction is direct, occurs under hypoxic conditions, and promotes its interaction with PIN1. Interacts with peptidyl-prolyl cis-trans isomerase PIN1; the interaction is direct, occurs under hypoxic conditions, and targets the protein to the mitochondrion by promoting interactions with the TOM complex. Interacts with mitochondrial circRNA mcPGK1 (via its 2nd stem-loop); the interaction is direct and targets the protein to the mitochondrion by promoting interactions with the TOM complex. Interacts with pyruvate dehydrogenase kinase PDK1; the interaction is direct, occurs under hypoxic conditions and leads to PDK1-mediated inhibition of pyruvate dehydrogenase complex activity

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5

• Hassan A.F. et al. Characterization of cDNAs coding for glucose phosphate isomerase and phosphoglycerate kinase in Chinese hamster ovary cell line CHO-K1 and identification of defects in R1.1.7, a glycolysis-deficient variant of CHO-K1. — Somat. Cell Mol. Genet. (1995)