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), EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)].
History
EC 5.4.2.4 created 1961 as EC 2.7.5.4, transferred 1984 to EC 5.4.2.4
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)
MCF: 
101925598(BPGM)
MMU: 
12183(Bpgm)
RNO: 
296973(Bpgm)
CGE: 
100757548(Bpgm)
HGL: 
101706859(Bpgm)
TUP: 
102496494(BPGM)
CFA: 
482704(BPGM)
AML: 
FCA: 
101095644(BPGM)
PTG: 
102952979(BPGM)
BTA: 
533785(BPGM)
BOM: 
PHD: 
102332772(BPGM)
CHX: 
102187916(BPGM)
CFR: 
102514048(BPGM)
BACU: 
LVE: 
103089210(BPGM)
ECB: 
100065115(BPGM)
MYB: 
102254057(BPGM)
MYD: 
102772643(BPGM)
PALE: 
102886645(BPGM)
MDO: 
100021814(BPGM)
SHR: 
100920227(BPGM)
OAA: 
100075920(BPGM)
GGA: 
418172(BPGM)
MGP: 
TGU: 
FAB: 
101817641(BPGM)
PHI: 
APLA: 
FPG: 
101915204(BPGM)
FCH: 
102046661(BPGM)
CLV: 
102089457(BPGM)
ASN: 
AMJ: 
102568684(BPGM)
PSS: 
102447629(BPGM)
CMY: 
102946921(BPGM)
ACS: 
PBI: 
XLA: 
XTR: 
549353(bpgm)
DRE: 
436903(bpgm)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102350982(BPGM)
CMK: 
103185559(bpgm)
 » 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
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
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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