Information on EC 5.4.2.4 - Bisphosphoglycerate mutase

New: Word Map on EC 5.4.2.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY hide
5.4.2.4
-
RECOMMENDED NAME
GeneOntology No.
Bisphosphoglycerate mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Rapoport-Luebering glycolytic shunt
-
-
SYSTEMATIC NAME
IUBMB Comments
3-Phospho-D-glycerate 1,2-phosphomutase
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)].
CAS REGISTRY NUMBER
COMMENTARY hide
37211-69-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
-
proposed mechanisms for the phosphatase and the synthase reactions involving residues His11 and Glu89
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-Diphosphoglycerate
2,3-Diphosphoglycerate
show the reaction diagram
2,3-Diphosphoglycerate
?
show the reaction diagram
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-Diphosphoglycerate
?
show the reaction diagram
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na2S2O4
-
stimulation
NaHSO3
-
stimulation
additional information
-
phosphoprotein, 1 mol per mol of subunit covalently bound, phosphoryl-group stable at alkaline pH, but liberated from the denatured protein at acidic pH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-diphosphoglycerate
-
product inhibition
2,4,6-Trinitrobenzenesulfonate
2-phosphoglycerate
-
-
2-Phosphoglycolate
-
-
3-phosphoglycerate
-
-
CH3COO-
-
-
Cl-
-
-
diphosphate
-
-
iodoacetamide
-
60% inhibition, protection by 2,3-diphosphoglycerate; protection by 2,3-diphosphoglycerate, or 3-phosphoglycerate, or 2-phosphoglycerate
N-ethylmaleimide
NaHSO3
-
-
Phytic acid
-
i.e. inositol hexaphosphate
potassium phosphate
-
-
SO42-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-phosphoglycerate
-
required, can be substituted by 3-phosphoglycerate
2-Phosphoglycolate
-
0.02 mM activates
3-phosphoglycerate
-
required, can be substituted by 2-phosphoglycerate
phosphoenolpyruvate
-
stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.0036
1,3-diphosphoglycerate
0.0024 - 0.583
2,3-diphosphoglycerate
additional information
additional information
-
kinetic parameters
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6 - 23.4
1,3-diphosphoglycerate
0.0037 - 0.152
2,3-diphosphoglycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.56
-
-
0.978
-
-
5.61
-
-
10.1
-
-
15
-
BPMG purified from diabetic patients
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
placental labyrinthine trophoblast, located at the maternal-placental interface
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
SDS-PAGE, mass spectrometry
54000
-
gel filtration
56500
-
gel filtration, sedimentation equilibrium centrifugation
60000
-
gel filtration
63000
-
sedimentation equilibrium centrifugation
120000
-
ultracentrifugation, cyanogen bromide cleavage, tryptic digestion
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 28000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
glycosylation at L158 leads to inactivation in diabetic patients
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.5 A, crystals have a rod-shaped morphology
-
co-crystallized with 2,3-bisphosphoglycerate. Enzyme conformation continuously changes during the different states of the reaction with in line phosphoryl transfer mechanism
-
hanging drop vapor diffusion method, using 18-22% (w/v) PEG 6K, 100 mM HEPES pH 6.8-7.2, at 17C
-
preliminary x-ray diffraction data
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
peak II enzyme stable, peak I and peak III enzyme 46% and 80% loss of activity in 10 min, respectively
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, concentrated solutions or 4C, 5 mM glycylglycine, pH 7.5, 0.5 mM EDTA, 2.5 mg/ml bovine serum albumin, 2 months, 30% loss of activity
-
-80C stable for up to 1 month
-
-80C, precipitated with ammonium sulfate, 3 months stable
-
-80C, sodium phosphate buffer, 20% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of EC 5.4.2.1 (phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase), three activities in one enzyme protein
expressed in Escherichia coli
-
mutant Arg89Cys
-
Ni-Speharose column chromatography
-
no bisphosphoglycerate phosphatase activity
-
purified from erythrocytes of diabetic patients
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of wild-type and mutants in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is about one third lower in placentae of insulin-like growth factor II heterozygote knockout mice compared to wild type
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E89G
-
construction of mutants with shortened chains and a mutant with Arg89Gly or Arg89Ser
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
BPGM deficiency can cause erythrocytosis