Bisphosphoglycerate mutase

bisphosphoglycerate mutase
Bisphosphoglycerate mutase homodimer, Human
Identifiers
EC no.5.4.2.4
CAS no.37211-69-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
2,3-bisphosphoglycerate mutase
Crystallographic structure of dimeric human bisphosphoglycerate mutase.[1]
Identifiers
SymbolBPGM
NCBI gene669
HGNC1093
OMIM222800
RefSeqNM_001724
UniProtP07738
Other data
EC number5.4.2.4
LocusChr. 7 q31-q34
Search for
StructuresSwiss-model
DomainsInterPro

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.

  1. ^ 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.
  2. ^ 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.

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