Information on EC 3.1.3.13 - bisphosphoglycerate phosphatase

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
3.1.3.13
-
RECOMMENDED NAME
GeneOntology No.
bisphosphoglycerate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycolysis / Gluconeogenesis
-
Rapoport-Luebering glycolytic shunt
-
SYSTEMATIC NAME
IUBMB Comments
2,3-bisphospho-D-glycerate 2-phosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2,3-bisphosphoglycerate phosphatase
-
-
-
-
2,3-diphosphoglycerate phosphatase
-
-
-
-
2,3-diphosphoglycerate phosphatase
P07738
-
2,3-diphosphoglyceric acid phosphatase
-
-
-
-
diphosphoglycerate phosphatase
-
-
-
-
glycerate-2,3-diphosphate phosphatase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9033-04-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme with inherent 3-phosphoglycerate mutase activity
-
-
Manually annotated by BRENDA team
enzyme with inherent 3-phosphoglycerate mutase activity
-
-
Manually annotated by BRENDA team
enzyme possesses phosphoglycerate mutase activity
-
-
Manually annotated by BRENDA team
enzyme with 3 activities: 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase
-
-
Manually annotated by BRENDA team
enzyme with inherent 3-phosphoglycerate mutase activity
-
-
Manually annotated by BRENDA team
EC 3.1.3.13 and EC 5.4.2.4 are associated in one protein
-
-
Manually annotated by BRENDA team
enzyme possesses activity of EC 5.4.2.1 and EC 3.1.3.13
-
-
Manually annotated by BRENDA team
enzyme with 3 activities: EC 3.1.3.13, EC 5.4.2.1, EC 5.4.2.4
-
-
Manually annotated by BRENDA team
phosphoglyceromutase/phosphatase
-
-
Manually annotated by BRENDA team
enzyme with inherent 3-phosphoglycerate mutase activity
-
-
Manually annotated by BRENDA team
enzyme with two activities: EC 5.4.2.4, EC 3.1.3.13
-
-
Manually annotated by BRENDA team
enzyme V-A with 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase in the ratio 0.1:0.06:1000; enzyme V-B with 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase in the ratio 40:0.3:1000
-
-
Manually annotated by BRENDA team
enzyme with 3 activities: 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase in the ratio: 40:0.3:1000
-
-
Manually annotated by BRENDA team
enzyme with 3 activities: 2,3-diphosphoglyceromutase, EC 5.4.2.4, 2,3-bisphosphoglycerate phosphatase, EC 3.1.3.13, and phosphoglyceromutase, EC 5.4.2.1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
P07738
the trifunctional enzyme regulates the level of 2,3-bisphosphoglycerate in red blood cells, the 2,3-bisphosphoglycerate phosphatase activity is responsible for rapid decline of 2,3-bisphosphoglycerate from storage in erythrocytes following fall of pH to limit the release of hemoglobin to blood
additional information
P07738
the erythrocytic enzyme is trifunctional exhibiting 2,3-diphosphoglycerate phosphatase, synthase, and mutase activities, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
-
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
-
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
-
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
ir
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
3-phospho-D-glycerate + phosphate
show the reaction diagram
-
-
-
-
?
2,3-bisphospho-D-glycerate + H2O
?
show the reaction diagram
-
the substrate is a heterotropic allosteric effector of oxygen-binding by hemoglobin
-
-
-
2,3-bisphospho-D-glycerate + H2O
?
show the reaction diagram
-
the substrate attenuates the binding of oxygen to deoxyhemoglobin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-bisphospho-D-glycerate + H2O
?
show the reaction diagram
-
the substrate is a heterotropic allosteric effector of oxygen-binding by hemoglobin
-
-
-
2,3-bisphospho-D-glycerate + H2O
?
show the reaction diagram
-
the substrate attenuates the binding of oxygen to deoxyhemoglobin
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cl-
-
activation in presence of 2-phosphoglycerate
Cl-
-
activation
diphosphate
-
stimulation in presence of NaCl
diphosphate
-
slight activation
diphosphate
-
-
diphosphate
-
stimulation
Dithionite
-
stimulation
Hg2+
-
activation of enzyme from skeletal muscle
Hg2+
-
no activation of kidney enzyme
HSO3-
-
stimulation
HSO3-
-
stimulation in presence of KCl
HSO3-
-
stimulation in presence of NaCl
HSO3-
-
-
HSO3-
-
activation
NH4VO3
-
activation by metavanadate
phosphate
-
activation in vivo
phosphate
-
activation up to 50 mM, inhibition above
SO32-
-
stimulation in presence of NaCl
SO32-
-
stimulation
VO43-
-
activation by orthovanadate
VO43-
-
activation by orthovanadate
HV2O73-
-
activation by divanadate
additional information
-
no activation by Hg2+, Zn2+, Cu2+, Ag+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-dipyridyl
-
slight inhibition
2-phosphoglycerate
-
-
2-phosphoglycerate
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
-
diphosphate
-
-
Hg2+
-
inhibition of enzyme from uterus
Hg2+
-
inhibition of enzyme from cardiac muscle
Inositol hexaphosphate
-
-
iodoacetate
-
-
N-ethylmaleimide
-
-
p-hydroxymercuribenzoate
-
-
Phenylglyoxal
-
-
phosphate
-
inhibition above 50 mM
tetrathionate
-
-
Trinitrobenzenesulfonate
-
-
Trinitrobenzenesulfonate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Phosphoglycolate
-
activation
2-Phosphoglycolate
-
activation
2-Phosphoglycolate
-
activation, Km: 0.479 mM
2-Phosphoglycolate
-
activation
2-Phosphoglycolate
-
no activation in vivo
2-Phosphoglycolate
-
activation
acetate
-
activation in presence of 2-phosphoglycerate
glycine
-
activation
N-[tris(hydroxymethyl)methyl-2-amino]ethanesulfonate
-
activation in presence of 2-phosphoglycerate
-
phosphoenolpyruvate
-
stimulation
Taurine
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000065
-
2,3-bisphosphoglycerate
-
-
0.00008
-
2,3-bisphosphoglycerate
-
pH 7.5, 25C, 0.1 M KCl, phosphate-activated
0.0025
-
2,3-bisphosphoglycerate
-
sodium TES buffer, pH 7.5, 25C
0.0028
-
2,3-bisphosphoglycerate
-
-
0.06
-
2,3-bisphosphoglycerate
-
-
0.082
-
2,3-bisphosphoglycerate
-
-
0.22
-
2,3-bisphosphoglycerate
-
-
0.33
-
2,3-bisphosphoglycerate
-
-
0.384
-
2,3-bisphosphoglycerate
-
in vivo
1.8
-
2,3-bisphosphoglycerate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0333
-
2,3-bisphosphoglycerate
-
-
2.6
-
2,3-bisphosphoglycerate
-
at 25C
5.95
-
2,3-bisphosphoglycerate
-
at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0073
-
-
-
0.34
-
-
-
1.7
-
-
-
9.3
-
-
-
39.7
-
-
-
515
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
-
-
6.8
-
-
-
7
-
P07738
assay at
7.5
-
-
-
additional information
-
-
independent of pH
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
-
-
5.7
8.5
-
less than 50% of maximal activity above and below
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
56000
-
-
gel filtration, ultracentrifugation
56000
-
-
enzyme V-B, gel filtration
60000
-
-
gel filtration
63000
-
-
sedimentation equilibrium centrifugation
65000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 28500, SDS-PAGE
dimer
-
2 * 28600, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 27000, enzyme V-B, SDS-PAGE
dimer
-
2 * 28000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, 17C, mixed with well solution consisting of 18-22% PEG 6000, 100 mM HEPES, pH 6.8-7.2, 1 week, X-ray diffraction structure determination and analysis at 1.94 A resolution
P07738
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
inactivation below
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
50
-
inactivation
49
-
-
4 min, 50% inactivation
50
-
-
4 min, complete inactivation, in presence of Hg2+ and 2,3-diphosphoglycerate 90% activity retained after 5 min
65
-
-
presence of 20 mM 2,3-bisphosphoglycerate, 15 min, 50% inactivation
70
-
-
complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
labile in dilute solutions
-
presence of glycerol essential
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, ammonium sulfate precipitate, at least 3 months stable
-
-80C, 10 mM triethanolamine-HCl buffer, pH 7.0, 1 mM EDTA, 0.32 mM dithiothreitol, 20% v/v glycerol
-
4C, 1 month stable
-
frozen, long-term storage
-
-20C, at least 1 month stable
-
0C, several weeks stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)
P07738
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
P07738
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
-
promotion of the accumulation of 2,3-diphosphoglycerate in erythrocytes by inhibition of EC 3.1.3.13