BPGM cDNA Clone – 2,3-Bisphosphoglycerate Mutase (Human)

2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2009]

BPGM: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD). A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.

Protein type: Isomerase; EC 5.4.2.4; EC 3.1.3.13; Phosphatase (non-protein); EC 5.4.2.11; Carbohydrate Metabolism - glycolysis and gluconeogenesis

Chromosomal Location of Human Ortholog: 7q33

Cellular Component: cytosol

Molecular Function: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; bisphosphoglycerate mutase activity

Biological Process: gluconeogenesis; glucose metabolic process; glycolysis; regulation of pentose-phosphate shunt; respiratory gaseous exchange

Disease: Bisphosphoglycerate Mutase Deficiency