Phosphoglycerate kinase (None)

Phosphoglycerate kinase (PGK) is a key enzyme involved in cellular energy metabolism, catalyzing a critical step in glycolysis. It facilitates the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP, generating 3-phosphoglycerate and ATP. Beyond glycolysis, PGK participates in gluconeogenesis and has been identified as a "moonlighting" protein with roles in pathogenesis, nucleic acid interactions, tumorigenesis progression, cell death regulation, and viral replication. Humans express two isoforms: PGK1 and PGK2. Deficiencies/mutations can cause rare inherited disorders characterized by hemolytic anemia or neurological symptoms.

Catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP, generating 3-phosphoglycerate and ATP. Orients substrates favorably for efficient phosphate transfer and stabilizes transition states during catalysis. Domain closure upon dual substrate binding creates an isolated environment optimal for reaction completion.