ENZYME entry: EC 5.4.2.4

Accepted Name
Bisphosphoglycerate mutase.
Alternative Name(s)
2,3-bisphosphoglycerate mutase.
2,3-bisphosphoglycerate synthase.
2,3-diphosphoglycerate mutase.
Bisphosphoglycerate synthase.
BPGM.
Diphosphoglycerate mutase.
Diphosphoglyceromutase.
Glycerate phosphomutase.
Reaction catalysed
3-phospho-D-glyceroyl phosphate <=> 2,3-bisphospho-D-glycerate
Comment(s)
  • In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate.
  • The latter is rephosphorylated by the enzyme to yield 2,3- diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate.
  • Also catalyzes, slowly, the reactions of EC 3.1.3.13 and EC 5.4.2.1.
  • Formerly EC 2.7.5.4.
Cross-references
PROSITEPDOC00158
BRENDA5.4.2.4
EC2PDB5.4.2.4
ExplorEnz5.4.2.4
PRIAM enzyme-specific profiles5.4.2.4
KEGG Ligand Database for Enzyme Nomenclature5.4.2.4
IUBMB Enzyme Nomenclature5.4.2.4
IntEnz5.4.2.4
MEDLINEFind literature relating to 5.4.2.4
MetaCyc5.4.2.4
UniProtKB/Swiss-Prot
Q3SZ62, PGAM1_BOVIN;  Q5ZLN1, PGAM1_CHICK;  P18669, PGAM1_HUMAN;  
Q9DBJ1, PGAM1_MOUSE;  Q5RFB8, PGAM1_PONAB;  P25113, PGAM1_RAT;  
Q32KV0, PGAM2_BOVIN;  P15259, PGAM2_HUMAN;  O70250, PGAM2_MOUSE;  
P16290, PGAM2_RAT;  Q8N0Y7, PGAM4_HUMAN;  Q8MKE8, PGAM4_PANTR;  
Q54NE6, PGAM_DICDI;  Q3T014, PMGE_BOVIN;  P07738, PMGE_HUMAN;  
Q4R6L7, PMGE_MACFA;  P15327, PMGE_MOUSE;  P07952, PMGE_RABIT;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.4.2.-
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