Phosphoglycerate kinase 1 (PGK1)

Phosphoglycerate kinase 1 (PGK1) is a highly conserved, ubiquitously expressed enzyme essential for cellular energy metabolism. It catalyzes the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate in glycolysis, generating ATP—the first substrate-level phosphorylation step of the glycolytic pathway[3][4][5]. Besides its canonical metabolic function, PGK1 is a moonlighting protein with diverse activities; it acts as a cofactor for DNA polymerase alpha in DNA replication, is secreted from tumor cells to modulate angiogenesis via angiostatin production, and functions as a protein kinase in mitochondria to regulate metabolic flux in response to oncogenic and hypoxic signaling[1][4][5]. Dysregulation of PGK1 is associated with inherited enzymopathies (including hemolytic anemia and myopathy) and is strongly implicated in cancer progression, where it supports tumor cell proliferation, invasion, and chemoresistance through metabolic and non-metabolic mechanisms[1][2][5].

Other names

PGKAMIG10OK/SW-cl.110PRP 2Cell migration-inducing gene 10 proteinPrimer recognition protein 2HEL-S-68pepididymis secretory sperm binding protein Li 68p

PGK1 generates ATP via phosphate transfer from 1,3-diphosphoglycerate to ADP. It inhibits the pyruvate dehydrogenase complex (via mitochondrial protein kinase activity on PDK1). PGK1 promotes or inhibits angiogenesis through the regulation of angiostatin formation.