KEGG   ENZYME: 5.4.2.4Help
Entry
EC 5.4.2.4                  Enzyme                                 

Name
bisphosphoglycerate mutase;
diphosphoglycerate mutase;
glycerate phosphomutase;
bisphosphoglycerate synthase;
bisphosphoglyceromutase;
biphosphoglycerate synthase;
diphosphoglyceric mutase;
2,3-diphosphoglycerate mutase;
phosphoglyceromutase;
2,3-diphosphoglycerate synthase;
DPGM;
2,3-bisphosphoglycerate mutase;
BPGM;
diphosphoglyceromutase;
2,3-diphosphoglyceromutase
Class
Isomerases;
Intramolecular transferases;
Phosphotransferases (phosphomutases)
BRITE hierarchy
Sysname
3-phospho-D-glycerate 1,2-phosphomutase
Reaction(IUBMB)
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate [RN:R01662]
Reaction(KEGG)
Substrate
3-phospho-D-glyceroyl phosphate [CPD:C00236]
Product
2,3-bisphospho-D-glycerate [CPD:C01159]
Comment
In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reactions of EC 3.1.3.13 (bisphosphoglycerate phosphatase) and EC 5.4.2.1 (phosphoglycerate mutase).
Pathway
Glycolysis / Gluconeogenesis
Orthology
K01837  
bisphosphoglycerate mutase
Genes
HSA: 
669(BPGM)
PTR: 
463746(BPGM)
PPS: 
100967755(BPGM)
GGO: 
101148078(BPGM)
PON: 
100445966(BPGM)
MCC: 
706741(BPGM)
MMU: 
12183(Bpgm)
RNO: 
296973(Bpgm)
CFA: 
482704(BPGM)
AML: 
FCA: 
101095644(BPGM)
BTA: 
533785(BPGM)
ECB: 
MDO: 
SHR: 
100920227(BPGM)
OAA: 
GGA: 
418172(BPGM)
MGP: 
TGU: 
ACS: 
XLA: 
XTR: 
549353(bpgm)
DRE: 
436903(bpgm)
TRU: 
OLA: 
 » show all
Taxonomy
Reference
1
  Authors
Ray, W.J., Jr. and Peck, E.J., Jr.
  Title
Phosphomutases.
  Journal
In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
Reference
2  [PMID:5687724]
  Authors
Rose ZB.
  Title
The purification and properties of diphosphoglycerate mutase from human erythrocytes.
  Journal
J. Biol. Chem. 243 (1968) 4810-20.
  Organism
Homo sapiens [GN:hsa]
Reference
3  [PMID:6255773]
  Authors
Rose ZB.
  Title
The enzymology of 2,3-bisphosphoglycerate.
  Journal
Adv. Enzymol. Relat. Areas. Mol. Biol. 51 (1980) 211-53.
  Organism
Homo sapiens [GN:hsa]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37211-69-1

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