Information on EC 3.1.3.80 - 2,3-bisphosphoglycerate 3-phosphatase

for references in articles please use BRENDA:EC3.1.3.80
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.80
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RECOMMENDED NAME
GeneOntology No.
2,3-bisphosphoglycerate 3-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Rapoport-Luebering glycolytic shunt
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Glycolysis / Gluconeogenesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
2,3-bisphospho-D-glycerate 3-phosphohydrolase
This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 5.4.2.11/EC 5.4.2.12 [phosphoglycerate mutases (2,3-diphosphoglycerate-dependent and independent)] and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate [1]. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ax2 wild-type background
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-bisphospho-D-glycerate + H2O
2-phospho-D-glycerate + phosphate
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-bisphospho-D-glycerate + H2O
2-phospho-D-glycerate + phosphate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
2,3-bisphospho-D-glycerate
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phosphatase activity of deglycosylated human HsMIPP1 protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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recombinant human HsMIPP1 protein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.3
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recombinant human HsMIPP1 protein, about 80% of maximal activity at pH 5, about 50% of maximal activity at pH 7.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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recombinant human HsMIPP1 protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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active at 4°C, more slowly than at 37°C, clinical relevance, significance of MIPP1 protein to contribute to the depletion of 2,3-bisphospho-D-glycerate during erythrocyte storage
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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human, recombinant HsMIPP1 protein, after treatment with endoglycosidase, the protein migrates with a lower apparent size
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
electroporation of Ax2 cells with the plasmid pJSK166, generated by cloning the full coding sequence into the extrachromosomal expression vector pRHI8
expressed in Escherichia coli
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expressed in Escherichia coli, human recombinant HsMIPP1 protein with a C-terminal myc-poly(His) epitope tag by using the Pichia pastoris expression system
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T27G
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mutant of recombinant chicken MIPP1 protein, more than 95% lower activity than wild-type enzyme
H89A
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mutant of recombinant HsMIPP1 protein, 1% of the 2,3-bisphospho-D-glycerate phophatase activity of the wild-type enzyme