Bisphosphoglycerate mutase (BPGM)

Bisphosphoglycerate mutase (BPGM) is an erythrocyte- and placental-specific enzyme that catalyzes the synthesis and hydrolysis of 2,3-bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. Through regulation of 2,3-BPG levels, BPGM decreases hemoglobin’s oxygen affinity and promotes oxygen release to tissues. BPGM is central to the Rapoport-Luebering pathway, and its deficiency leads to altered oxygen delivery and erythrocytosis. The enzyme is a dimer with active sites at each monomer and functions through a nucleophilic mechanism involving key histidine residues. Modulation of BPGM activity has therapeutic interest, especially in conditions like sickle cell disease, where 2,3-BPG concentrations impact disease severity[1][3][4][5].

Other names

2,3-bisphosphoglycerate mutaseDPGMerythrocyte 2,3-bisphosphoglycerate mutase2,3-bisphosphoglycerate synthase2,3-diphosphoglycerate mutaseBPG-dependent PGAMECYT8testis secretory sperm-binding protein Li 202a

Allosteric modulation of BPGM enzymatic activity; Inhibition of phosphatase activity (e.g., by citrate)