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 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
ec01100  Metabolic pathways
Orthology
K01837  bisphosphoglycerate/phosphoglycerate mutase
Genes
HSA: 669(BPGM)
PTR: 463746(BPGM)
PPS: 100967755(BPGM)
GGO: 101148078(BPGM)
PON: 100445966(BPGM)
NLE: 100586238(BPGM)
MCC: 706741(BPGM)
MCF: 101925598(BPGM)
CSAB: 103226934(BPGM)
RRO: 104655279(BPGM) 104657786 104659152
RBB: 108522539(BPGM)
CJC: 100386672(BPGM)
SBQ: 101031409(BPGM)
MMU: 12183(Bpgm)
RNO: 296973(Bpgm)
CGE: 100757548(Bpgm)
NGI: 103726061(Bpgm)
HGL: 101706859(Bpgm)
CCAN: 109688796
OCU: 100009096(BPGM)
TUP: 102496494(BPGM)
CFA: 482704(BPGM)
AML: 100479620(BPGM)
UMR: 103678255(BPGM)
ORO: 101365932(BPGM)
FCA: 101095644(BPGM)
PTG: 102952979(BPGM)
AJU: 106975708(BPGM)
BTA: 533785(BPGM)
BIU: 109557654(BPGM)
PHD: 102332772(BPGM)
CHX: 102187916(BPGM)
OAS: 101121089(BPGM)
SSC: 106506774(BPGM)
CFR: 102514048(BPGM)
CDK: 105085404(BPGM)
BACU: 103009787(BPGM) 103015640
LVE: 103089210(BPGM)
OOR: 101286738 101287641(BPGM)
ECB: 100065115(BPGM)
EPZ: 103551316(BPGM)
EAI: 106830008(BPGM)
MYB: 102254057(BPGM)
MYD: 102772643(BPGM)
HAI: 109389371(BPGM)
RSS: 109457774(BPGM)
PALE: 102886645(BPGM)
LAV: 100673907(BPGM)
TMU: 101360256
MDO: 100021814(BPGM)
SHR: 100920227(BPGM)
OAA: 100075920(BPGM)
GGA: 418172(BPGM)
MGP: 100546129(BPGM)
CJO: 107314945(BPGM)
APLA: 101803151(BPGM)
ACYG: 106030917(BPGM)
TGU: 100224087
GFR: 102033451(BPGM)
FAB: 101817641(BPGM)
PHI: 102108959(BPGM)
PMAJ: 107204390(BPGM)
CCAE: 111928156(BPGM)
CCW: 104692259(BPGM)
FPG: 101915204(BPGM)
FCH: 102046661(BPGM)
CLV: 102089457(BPGM)
EGZ: 104134376(BPGM)
AAM: 106488955(BPGM)
ASN: 102373803(BPGM)
AMJ: 102568684(BPGM)
PSS: 102447629(BPGM)
CMY: 102946921(BPGM)
CPIC: 101941911(BPGM)
ACS: 100564984(bpgm)
PVT: 110088825(BPGM)
PBI: 103062795(BPGM)
GJA: 107125358(BPGM)
XLA: 444102(bpgm.L) 444279(bpgm.S)
XTR: 549353(bpgm)
NPR: 108792024(BPGM)
DRE: 436903(bpgm)
SANH: 107661509
IPU: 108269072(bpgm)
AMEX: 103029505(bpgm)
TRU: 101074347(bpgm)
LCO: 104940663(bpgm)
NCC: 104946798(bpgm)
MZE: 101473870(bpgm)
OLA: 101172407(bpgm)
XMA: 102233730(bpgm)
PRET: 103465823(bpgm)
NFU: 107388481(bpgm)
KMR: 108229885(bpgm)
CSEM: 103380563(bpgm)
LCF: 108888560(bpgm)
SDU: 111229658(bpgm)
HCQ: 109530859(bpgm)
BPEC: 110169450(bpgm)
MALB: 109951197(bpgm)
SASA: 100196266(pmge) 106561646
ELS: 105021856(bpgm)
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 243:4810-20 (1968)
Reference
3  [PMID:6255773]
  Authors
Rose ZB.
  Title
The enzymology of 2,3-bisphosphoglycerate.
  Journal
Adv Enzymol Relat Areas Mol Biol 51:211-53 (1980)
Other DBs
ExplorEnz - The Enzyme Database: 5.4.2.4
IUBMB Enzyme Nomenclature: 5.4.2.4
ExPASy - ENZYME nomenclature database: 5.4.2.4
BRENDA, the Enzyme Database: 5.4.2.4
CAS: 37211-69-1

DBGET integrated database retrieval system