Bisphosphoglycerate mutase
| bisphosphoglycerate mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Bisphosphoglycerate mutase homodimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 5.4.2.4 | ||||||||
| CAS no. | 37211-69-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| 2,3-bisphosphoglycerate mutase | |||||||
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Crystallographic structure of dimeric human bisphosphoglycerate mutase. | |||||||
| Identifiers | |||||||
| Symbol | BPGM | ||||||
| NCBI gene | 669 | ||||||
| HGNC | 1093 | ||||||
| OMIM | 222800 | ||||||
| RefSeq | NM_001724 | ||||||
| UniProt | P07738 | ||||||
| Other data | |||||||
| EC number | 5.4.2.4 | ||||||
| Locus | Chr. 7 q31-q34 | ||||||
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Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme expressed in erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM has both a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent.