| 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 | ||||||||
| |||||||||
| 2,3-bisphosphoglycerate mutase | |||||||
|---|---|---|---|---|---|---|---|
 Crystallographic structure of dimeric human bisphosphoglycerate mutase.[1] | |||||||
| 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 | ||||||
| |||||||
Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme expressed in erythrocytes and placental cells.[2] It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has 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.
- ^ PDB: 1T8P; Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W (September 2004). "Crystal structure of human bisphosphoglycerate mutase". J. Biol. Chem. 279 (37): 39132–8. doi:10.1074/jbc.M405982200. PMID 15258155.
- ^ Pritlove DC, Gu M, Boyd CA, Randeva HS, Vatish M (August 2006). "Novel placental expression of 2,3-bisphosphoglycerate mutase". Placenta. 27 (8): 924–7. doi:10.1016/j.placenta.2005.08.010. PMID 16246416.