Entry
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 reaction of 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
ec00010 Glycolysis / Gluconeogenesis
Orthology
K01837 bisphosphoglycerate/phosphoglycerate mutase
Genes
RRO : 104655279(BPGM) 104657786
CJC : 100386672(BPGM) 128928554
DSP : 122099556(Bpgm) 122125320
NCAR : 124986309 124990814
PYU : 121028302(BPGM) 121031877
BTA : 112447087 533785(BPGM)
BOM : 102270409 102275256 102275503(BPGM)
BACU : 103009787(BPGM) 103015640
BMUS : 118891256 118901329(BPGM)
OOR : 101286738 101287641(BPGM)
LALB : 132516124 132524119(BPGM)
DLE : 111178164(BPGM) 111178314
PSIU : 116759523(BPGM) 116764955
NASI : 112392791 112394975(BPGM)
MMYO : 118666381(BPGM) 118676662
TACU : 119933341(BPGM) 119941805
CPEA : 104384749 104393436(BPGM)
XLA : 444102(bpgm.L) 444279(bpgm.S)
CAUA : 113043324 113066900
CGIB : 127946682 128014707
MASI : 127436034 127437701
SBIA : 133501972 133502515(bpgm)
PTAO : 133477980 133478226(bpgm)
SASA : 100196266(pmge) 106561646
STRU : 115152372 115197620
OGO : 124004499 124032856(bpgm)
ONE : 115109699(bpgm) 115115104
OMM : 135508996(bpgm) 135524081
SALP : 111952995 111962766
CCLU : 121531280 121577059
AANG : 118219313 118232037(bpgm)
AROT : 135245627 135259889
CCOG : 133119048 133135310
PSPA : 121318552 121319494
ARUT : 117415332 117419669
» show all
Taxonomy
Reference
1
Authors
Ray WJ Jr, Peck EJ Jr.
Title
Phosphomutases.
Journal
In: Boyer PD (ed). The Enzymes. 3rd ed. Vol. 6. 1972. p. 407-477.
Reference
Authors
Rose ZB.
Title
The purification and properties of diphosphoglycerate mutase from human erythrocytes.
Journal
J Biol Chem 243:4810-20 (1968)
Reference
Authors
Rose ZB.
Title
The enzymology of 2,3-bisphosphoglycerate.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 5.4.2.4
ExPASy - ENZYME nomenclature database: 5.4.2.4
BRENDA, the Enzyme Database: 5.4.2.4