bisphosphoglycerate mutase | |||||||||
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![]() 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.[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 | ||||||
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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.