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Information on EC 5.4.2.4 - Bisphosphoglycerate mutase and Organism(s) Homo sapiens

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.4 Bisphosphoglycerate mutase
IUBMB 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
The taxonomic range for the selected organisms is: Homo sapiens
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, 3-phospho-d-glycerate 1,2-phosphomutase, 2,3-diphosphoglycerate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-Bisphosphoglycerate mutase
-
-
-
-
2,3-bisphosphoglycerate mutase, erythrocyte
-
-
-
-
2,3-bisphosphoglycerate synthase
-
-
-
-
2,3-Diphosphoglycerate mutase
-
-
-
-
2,3-Diphosphoglycerate synthase
-
-
-
-
2,3-Diphosphoglyceromutase
-
-
-
-
Biphosphoglycerate synthase
-
-
-
-
bisphosphoglycerate mutase
Bisphosphoglyceromutase
-
-
-
-
BPG synthase
-
-
BPG-dependent PGAM
-
-
-
-
BPGAM
a trifunctional enzyme that possesses mutase, synthase and phosphatase activities
Diphosphoglycerate mutase
-
-
-
-
Diphosphoglyceric mutase
-
-
-
-
Diphosphoglyceromutase
-
-
-
-
DPGM
-
-
-
-
Glycerate phosphomutase
-
-
-
-
Phosphomutase, glycerate (phosphoglycerate cofactor)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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)].
CAS REGISTRY NUMBER
COMMENTARY hide
37211-69-1
-
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 SUBSTRATE
NATURAL PRODUCT
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trinitrobenzenesulfonate
2-Phosphoglycolate
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-
CH3COO-
-
-
Cl-
-
-
iodoacetamide
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60% inhibition, protection by 2,3-diphosphoglycerate; protection by 2,3-diphosphoglycerate, or 3-phosphoglycerate, or 2-phosphoglycerate
N-ethylmaleimide
NaHSO3
-
-
potassium phosphate
-
-
SO42-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.0036
1,3-diphosphoglycerate
0.0094 - 0.583
2,3-diphosphoglycerate
additional information
additional information
-
kinetic parameters
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037 - 0.152
2,3-diphosphoglycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.1
-
-
15
-
BPMG purified from diabetic patients
5.61
-
-
9.78
-
-
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme deletion disrupts PGAM1 activity and results in higher serine de novo synthesis flux
metabolism
physiological function
additional information
-
proposed mechanisms for the phosphatase and the synthase reactions involving residues His11 and Glu89
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PMGE_HUMAN
259
0
30005
Swiss-Prot
other Location (Reliability: 3)
PGAM1_HUMAN
254
0
28804
Swiss-Prot
other Location (Reliability: 2)
PGAM2_HUMAN
253
0
28766
Swiss-Prot
other Location (Reliability: 3)
PGAM4_HUMAN
254
0
28777
Swiss-Prot
other Location (Reliability: 2)
Q6P6D7_HUMAN
254
0
28820
TrEMBL
other Location (Reliability: 2)
Q6FHK8_HUMAN
254
0
28835
TrEMBL
other Location (Reliability: 2)
Q6FHU2_HUMAN
254
0
28804
TrEMBL
other Location (Reliability: 2)
Q59GR5_HUMAN
147
0
17326
TrEMBL
other Location (Reliability: 4)
C9JH23_HUMAN
78
0
9220
TrEMBL
other Location (Reliability: 3)
A4D2J6_HUMAN
252
0
28220
TrEMBL
other Location (Reliability: 3)
Q0D2Q6_HUMAN
254
0
28792
TrEMBL
other Location (Reliability: 2)
A0A024R782_HUMAN
259
0
30005
TrEMBL
other Location (Reliability: 3)
O00228_HUMAN
75
0
8573
TrEMBL
other Location (Reliability: 2)
Q53G35_HUMAN
254
0
28832
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
-
2 * 26500, SDS-PAGE
27200
-
2 * 27200, SDS-PAGE
29000
-
2 * 29000, SDS-PAGE
30000
SDS-PAGE, mass spectrometry
32000
-
2 * 32000, SDS-PAGE
54000
-
gel filtration
56500
-
gel filtration, sedimentation equilibrium centrifugation
60000
-
gel filtration
63000
-
sedimentation equilibrium centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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 17°C
preliminary x-ray diffraction data
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E89G
-
construction of mutants with shortened chains and a mutant with Arg89Gly or Arg89Ser
additional information
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
-20°C, concentrated solutions or 4°C, 5 mM glycylglycine, pH 7.5, 0.5 mM EDTA, 2.5 mg/ml bovine serum albumin, 2 months, 30% loss of activity
-
-80°C stable for up to 1 month
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-80°C, sodium phosphate buffer, 20% glycerol
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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
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expressed in Escherichia coli
-
mutant Arg89Cys
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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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
BPGM deficiency can cause erythrocytosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rose, Z.B.
The enzymology of 2,3-bisphosphoglycerate
Adv. Enzymol. Relat. Areas Mol. Biol.
51
211-253
1980
Homo sapiens
Manually annotated by BRENDA team
Ikura, K.; Narita, H.; Sasaki, R.; Chiba, H.
Immunochemical and enzymatic properties of bisphosphoglyceromutase/phosphatase and phosphoglyceromutase from human erythrocytes
Eur. J. Biochem.
89
23-31
1978
Homo sapiens
Manually annotated by BRENDA team
Hass, L.F.; Sheibley, R.H.; Kappel, W.K.; Miller, K.B.
A comparison of some of the physical and chemical properties of the phosphoglycerate mutases from human erythrocytes
Biochem. Biophys. Res. Commun.
72
976-983
1976
Homo sapiens
Manually annotated by BRENDA team
Ravel, P.; Craescus, C.T.; Arous, N.; Rosa, J.; Garel, M.C.
Critical Role of Human bisphosphoglycerate mutase Cys22 in the phosphatase activator-binding site
J. Biol. Chem.
272
14045-14050
1997
Homo sapiens
Manually annotated by BRENDA team
Calcin, M.C.; Blouquit, Y.; Garel, M.C.; Cohen-Solal, M.; Rosa, J.; Rosa, R.
Human bisphosphogycerate mutase expressed in E. coli: purification, characterization and structure studies
Biochimie
72
337-343
1990
Homo sapiens
Manually annotated by BRENDA team
Garel, M.C.; Lemarchandel, M.O.; Prehu, M.O.; Calvin, M.C.; Arous, N.; Rosa, R.; Rosa, J.
Natural and artificial mutants of the human 2,3-bisphosphoglycerate as a tool for the evaluation of structure-function relationship
Biomed. Biochim. Acta
49
166-171
1990
Homo sapiens
-
Manually annotated by BRENDA team
Garel, M.C.; Joulin, V.; Le Boulch, P.; Calvin, M.C.; Prehu, M.O.; Arous, N.; Longin, R.; Rosa, R.; Rosa, J.; Cohen-Solal, M.
Human bisphosphglycerate mutase. Expression in Escherichia coli and use of site-directed mutagenesis in the evaluation of the role of the carboxyl-terminal region in the enzymatic mechanism
J. Biol. Chem.
264
18966-18972
1989
Homo sapiens
Manually annotated by BRENDA team
Rosa, R.; Blouquit, Y.; Calvin, M.C.; Prome, D.; Prome, J.C.; Rosa, J.
Isolation, characterization, and structure of a mutant 89 ARG->Cys bisphosphoglycerate mutase. Implication of the active site in the mutation
J. Biol. Chem.
264
7837-7843
1989
Homo sapiens
Manually annotated by BRENDA team
Rosa, R.; Calvin, M.C.
Comparative effects of two sulfhydryl reagents on the activities of a multifunctional red cell enzyme: bisphosphoglycerate mutase
Biochem. Biophys. Res. Commun.
153
945-951
1988
Homo sapiens
Manually annotated by BRENDA team
Cherfils, J.; Rosa, R.; Garel, M.C.; Calvin, M.C.; Rosa, J.; Janin, J.
Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase
J. Mol. Biol.
20
269-270
1991
Homo sapiens
Manually annotated by BRENDA team
Rose, Z.B.; Whalen, R.G.
The phosphorylation of diphosphoglycerate mutase
J. Biol. Chem.
248
1513-1519
1973
Homo sapiens
Manually annotated by BRENDA team
Rose, Z.B.
Effects of salt and pH on the rate of erythrocyte diphosphoglycerate mutase
Arch. Biochem. Biophys.
158
903-910
1973
Homo sapiens
Manually annotated by BRENDA team
McPherson, A.
Crystallization of proteins from polyethylene glycol
J. Biol. Chem.
251
6300-6303
1976
Homo sapiens
Manually annotated by BRENDA team
Sasaki, R.; Ikura, K.; Sugimoto, E.; Chiba, H.
Purification of bisphosphoglyceromutase, 2,3-bisphosphoglycerate phosphatase and phosphoglyceromutase from human erthrocytes. Three enzyme activities in one protein
Eur. J. Biochem.
50
581-593
1975
Homo sapiens
Manually annotated by BRENDA team
Rose, Z.B.
2,3-Diphosphoglycerate mutase from human erythrocytes
Methods Enzymol.
42C
450-454
1975
Homo sapiens
Manually annotated by BRENDA team
Kappel, W.K.; Hass, L.F.
The isolation and partial characterization of diphosphoglycerate mutase from human erythrocytes
Biochemistry
15
290-295
1976
Homo sapiens
Manually annotated by BRENDA team
Ikura, K.; Sasaki, R.; Narita, H.; Sugimoto, E.; Chiba, H.
Multifunctional enzyme, bisphosphoglyceromutase/2,3-bisphosphoglycerate phosphatase/phosphoglyceromutase, from human erythrocytes. Evidence for a common active site
Eur. J. Biochem.
66
515-522
1976
Homo sapiens
Manually annotated by BRENDA team
Rosa, R.; Prehu, M.O.; Albrecht-Ellmer, K.; Calvin, M.C.
Partial characterization of the inactive mutant form of human red cell bisphosphoglyceromutase and comparison with an alkylated form
Biochim. Biophys. Acta
742
243-249
1983
Homo sapiens
Manually annotated by BRENDA team
Joulin, V.; Peduzzi, J.; Romeo, P.H.; Rosa, R.; Valentin, C.; Dubart, A.; Lapeyre, B.; Blouquit, Y.; Garel, M.C.; Goossens, M.; Rosa, J.; Cohen-Solal, M.
Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence
EMBO J.
5
2275-2283
1986
Homo sapiens
Manually annotated by BRENDA team
Fujita, T.; Suzuki, K.; Tada, T.; Yoshihara, Y.; Hamaoka, R.; Uchida, K.; Matuo, Y.; Sasaki, T.; Hanafusa, T.; Taniguchi, N.
Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro
J. Biochem.
124
1237-1244
1998
Homo sapiens
Manually annotated by BRENDA team
Hoyer, J.D.; Allen, S.L.; Beutler, E.; Kubik, K.; West, C.; Fairbanks, V.F.
Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency
Am. J. Hematol.
75
205-208
2004
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Wei, Z.; Bian, Q.; Cheng, Z.; Wan, M.; Liu, L.; Gong, W.
Crystal structure of human bisphosphoglycerate mutase
J. Biol. Chem.
279
39132-39138
2004
Homo sapiens (P07738), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Liu, L.; Wei, Z.; Cheng, Z.; Lin, Y.; Gong, W.
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase
J. Biol. Chem.
281
39642-39648
2006
Homo sapiens (P07738), Homo sapiens
Manually annotated by BRENDA team
Patterson, A.; Price, N.C.; Nairn, J.
Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding
Acta Crystallogr. Sect. F
66
1415-1420
2010
Homo sapiens (P07738), Homo sapiens
Manually annotated by BRENDA team
Bertrand, R.
Nitric oxide-mediated suppression of 2,3-bisphosphoglycerate synthesis: therapeutic relevance for environmental hypoxia and sickle cell disease
Med. Hypotheses
79
315-318
2012
Homo sapiens
Manually annotated by BRENDA team
Chu, W.T.; Zheng, Q.C.; Zhang, H.X.
Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation
Phys. Chem. Chem. Phys.
16
3946-3954
2014
Homo sapiens
Manually annotated by BRENDA team
Oslund, R.C.; Su, X.; Haugbro, M.; Kee, J.M.; Esposito, M.; David, Y.; Wang, B.; Ge, E.; Perlman, D.H.; Kang, Y.; Muir, T.W.; Rabinowitz, J.D.
Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate
Nat. Chem. Biol.
13
1081-1087
2017
Homo sapiens
Manually annotated by BRENDA team