BPGM

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.

2,3-bisphosphoglycerate mutase

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 5.4.2.11) activity.

Carbohydrate derivative catabolic process Source: Reactome
Carbohydrate metabolic process Source: ProtInc
Erythrocyte development Source: Ensembl
Glycolytic process Source: UniProtKB-KW
Respiratory gaseous exchange by respiratory system Source: ProtInc

Cytosol; Extracellular exosome

Erythrocytosis, familial, 8 (ECYT8): An autosomal recessive disorder characterized by elevated serum hemoglobin and hematocrit, and biphosphoglycerate mutase deficiency. ECYT8 affected individuals manifest hemolytic anemia and splenomegaly.

Glycation of Lys-159 in diabetic patients inactivates the enzyme.