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Information on EC 5.4.2.4 - Bisphosphoglycerate mutase
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5.4.2.4 Bisphosphoglycerate mutaseIUBMB Comments
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)].
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Word Map
- 5.4.2.4
-
phosphofructokinase
-
monophosphoglycerates
- 1,3-bisphosphoglycerate
- erythrocytosis
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hemolysate
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erythrocyte-specific
- 2-phosphoglycolate
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
bisphosphoglycerate mutase, 2,3-bisphosphoglycerate mutase, diphosphoglycerate mutase, bisphosphoglyceromutase, 2,3-bisphosphoglycerate synthase, 2,3-diphosphoglycerate mutase, diphosphoglyceromutase, bpg synthase, 2,3-diphosphoglyceromutase, 3-phospho-d-glycerate 1,2-phosphomutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Bisphosphoglycerate mutase
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2,3-bisphosphoglycerate mutase, erythrocyte
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2,3-bisphosphoglycerate synthase
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2,3-Diphosphoglycerate mutase
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2,3-Diphosphoglycerate synthase
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2,3-Diphosphoglyceromutase
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Biphosphoglycerate synthase
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bisphosphoglycerate mutase
Bisphosphoglyceromutase
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BPG-dependent PGAM
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BPGAM
a trifunctional enzyme that possesses mutase, synthase and phosphatase activities
BPGM
Diphosphoglycerate mutase
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Diphosphoglyceric mutase
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Diphosphoglyceromutase
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DPGM
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EC 2.7.5.4
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formerly
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Glycerate phosphomutase
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Phosphomutase, glycerate (phosphoglycerate cofactor)
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BPGM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
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intramolecular, phosphate group
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isomerization
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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 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)].
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CAS REGISTRY NUMBER
COMMENTARY
37211-69-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-Diphosphoglycerate
2,3-Diphosphoglycerate
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the enzyme has additional activities of EC 5.4.2.1(phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase)
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?
1,3-Diphosphoglycerate
2,3-Diphosphoglycerate
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the enzyme has additional activities of EC 5.4.2.1(phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase)
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?
1,3-Diphosphoglycerate
2,3-Diphosphoglycerate
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multifunctional enzyme for synthesis and degradation of 2,3-diphosphoglycerate
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2,3-Diphosphoglycerate
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multifunctional enzyme for synthesis and degradation of 2,3-diphosphoglycerte, additional activities are diphosphoglycerate phosphatase and phosphoglycerate mutase
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2,3-Diphosphoglycerate
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in red blood cells 2,3-diphosphoglycerate is the main allosteric effector of hemoglobin, shifting the equilibrium between the oxy and deoxy conformations of hemoglobin preferentially stabilizing the unliganded form. 2,3-Diphosphoglycerate also promotes the polymerization of deoxyhemoglobin in sickle cell disease
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?
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
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?
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
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BPGM plays a pivotal role in the dissociation of oxygen from hemoglobin via 2,3-bisphospho-D-glycerate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-Diphosphoglycerate
?
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multifunctional enzyme for synthesis and degradation of 2,3-diphosphoglycerte, additional activities are diphosphoglycerate phosphatase and phosphoglycerate mutase
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?
2,3-Diphosphoglycerate
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in red blood cells 2,3-diphosphoglycerate is the main allosteric effector of hemoglobin, shifting the equilibrium between the oxy and deoxy conformations of hemoglobin preferentially stabilizing the unliganded form. 2,3-Diphosphoglycerate also promotes the polymerization of deoxyhemoglobin in sickle cell disease
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?
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
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?
3-phospho-D-glyceroyl phosphate
2,3-bisphospho-D-glycerate
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BPGM plays a pivotal role in the dissociation of oxygen from hemoglobin via 2,3-bisphospho-D-glycerate
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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phosphoprotein, 1 mol per mol of subunit covalently bound, phosphoryl-group stable at alkaline pH, but liberated from the denatured protein at acidic pH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
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60% inhibition, protection by 2,3-diphosphoglycerate; protection by 2,3-diphosphoglycerate, or 3-phosphoglycerate, or 2-phosphoglycerate
2,4,6-Trinitrobenzenesulfonate
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amino-specific reagent, protection by 2,3-diphosphoglycerate or 1,3-diphosphoglycerate
N-ethylmaleimide
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protection by 2,3-diphosphoglycerate, not by 3-phosphoglycerate or 2-phosphoglycerate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia
Bisphosphoglycerate Mutase Deficiency Protects against Cerebral Malaria and Severe Malaria-Induced Anemia.
Anemia, Hemolytic
[Congenital non-spherocytic hemolytic anemia by 2,3-diphosphoglycerate mutase deficiency of the erythrocytes in early infancy]
Anemia, Hemolytic
[Metabolic aspects of the erythrocytes in a case of congenital non-spherocytic hemolytic anemia with probable of 2,3-diphosphoglyceromutase deficiency]
Anemia, Refractory
[Enzyme deficiencies of blood cells in bone marrow insufficiency (author's transl]
bisphosphoglycerate mutase deficiency
Bisphosphoglycerate Mutase Deficiency Protects against Cerebral Malaria and Severe Malaria-Induced Anemia.
bisphosphoglycerate mutase deficiency
Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency.
bisphosphoglycerate mutase deficiency
Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency.
bisphosphoglycerate mutase deficiency
Glycerated hemoglobin alpha 2 beta 2(82) (EF6) N-epsilon-glyceryllysine: a new post-translational modification occurring in erythrocyte bisphosphoglyceromutase deficiency.
bisphosphoglycerate mutase deficiency
Glycerated hemoglobin, alpha 2A beta 2(82) (EF6) N epsilon-glyceryllysine. A new post-translational modification occurring in erythrocyte bisphosphoglyceromutase deficiency.
bisphosphoglycerate mutase deficiency
Red cell enzymopathies as a model of inborn errors of metabolism.
bisphosphoglycerate mutase deficiency
[2,3-diphosphoglycerate metabolism and 2,3-diphosphoglycerate mutase deficiency in erythrocytes]
bisphosphoglycerate mutase deficiency
[Congenital non-spherocytic hemolytic anemia by 2,3-diphosphoglycerate mutase deficiency of the erythrocytes in early infancy]
bisphosphoglycerate mutase deficiency
[Diphosphoglyceromutase deficiency: new cases associated with erythrocytosis]
bisphosphoglycerate mutase deficiency
[Familial diphosphoglycerate mutase deficiency: hematological and biochemical study]
bisphosphoglycerate mutase deficiency
[Metabolic aspects of the erythrocytes in a case of congenital non-spherocytic hemolytic anemia with probable of 2,3-diphosphoglyceromutase deficiency]
Leukemia, Erythroblastic, Acute
Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA.
Malaria
The use of enzymopathic human red cells in the study of malarial parasite glucose metabolism.
Malaria, Cerebral
Bisphosphoglycerate Mutase Deficiency Protects against Cerebral Malaria and Severe Malaria-Induced Anemia.
Malaria, Falciparum
The use of enzymopathic human red cells in the study of malarial parasite glucose metabolism.
Neoplasms
Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas.
Polycythemia
Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency.
Polycythemia
Uniparental disomy (UPD) of a novel bisphosphoglycerate mutase (BPGM) mutation leading to erythrocytosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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placental labyrinthine trophoblast, located at the maternal-placental interface
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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enzyme deletion disrupts PGAM1 activity and results in higher serine de novo synthesis flux
metabolism
physiological function
additional information
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proposed mechanisms for the phosphatase and the synthase reactions involving residues His11 and Glu89
metabolism
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NO may suppress 2,3-bisphospho-D-glycerate production by (1) inhibiting glyceraldehyde-3-phosphate dehydrogenase, the most critical glycolytic enzyme for the bioavailability of 1,3-bisphosphoglycerate, and to a lesser extent by (2) associated pH changes in the deoxy-hemoglobin-catalyzed depletion of nitrite, a metabolic reservoir of NO
metabolism
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the main activity of the enzyme is synthase (EC 5.4.2.4), converting 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate. The second activity is mutase (phosphoglycerate mutase, EC 5.4.2.1), catalyzing the interconversion between 2-phosphoglycerate and 3-phosphoglycerate. The third activity is phosphatase (S-succinylglutathione hydrolase, EC 3.1.3.13), hydrolyzing 2,3-bisphosphoglycerate to 3-phosphoglycerate or 2-phosphoglycerate and phosphate
metabolism
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the enzyme primarily impacts 3-phosphoglycerate concentration and thereby serine pathway flux
physiological function
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bisphosphoglycerate mutase is a multi-activity enzyme. Its main function is to synthesize the 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin, the enzyme regulates 2,3-bisphosphoglycerate levels, quantum mechanics/molecular mechanics simulations based on the metadynamics and umbrella sampling simulations, detailed overview
physiological function
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the enzyme is responsible for biosynthesis of 2,3-bisphospho-D-glycerate, which is an enhancer of oxygen off-loading from hemoglobin. It is very sensitive to changes in glycolytic rates because its synthesis by BPG synthase is dependent on the availability of the glycolytic intermediate 1,3-bisphosphoglycerate, metabolic enzyme regulation, overview
Show AA Sequence and Transmembrane Helices (1912 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
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ultracentrifugation, cyanogen bromide cleavage, tryptic digestion
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-crystallized with 2,3-bisphosphogl