Any feedback?
Information on EC 3.1.3.80 - 2,3-bisphosphoglycerate 3-phosphatase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.1.3.80Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.3.80 2,3-bisphosphoglycerate 3-phosphataseIUBMB Comments
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 . The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).
Specify your search results
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
2,3-BPG 3-phosphatase, DdMipp1, HsMIPP1 protein, MIPP1 protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-BPG 3-phosphatase
-
-
-
-
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).
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
2,3-bisphospho-D-glycerate + H2O
2-phospho-D-glycerate + phosphate
-
2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, additional bisphosphoglycerate phosphatase identified, glycolytic pathway can bypass the formation of 3-phospho-D-glycerate, biological significance of the Rapoport-Luebering shunt, physiologically relevant regulation of cellular 2,3-bisphospho-D-glycerate content
-
-
?
2,3-bisphospho-D-glycerate + H2O
2-phospho-D-glycerate + phosphate
-
2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, additional bisphosphoglycerate phosphatase identified, glycolytic pathway can bypass the formation of 3-phospho-D-glycerate, biological significance of the Rapoport-Luebering shunt
-
-
?
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-bisphospho-D-glycerate + H2O
2-phospho-D-glycerate + phosphate
-
2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, additional bisphosphoglycerate phosphatase identified, glycolytic pathway can bypass the formation of 3-phospho-D-glycerate, biological significance of the Rapoport-Luebering shunt, physiologically relevant regulation of cellular 2,3-bisphospho-D-glycerate content
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.61
2,3-bisphospho-D-glycerate
-
phosphatase activity of deglycosylated human HsMIPP1 protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
identification of a second enzyme component of the Rapoport-Luebering shunt, separate 2,3-bisphosphoglycerate phosphatase activity, quantification of recombinant human HsMIPP1 activity in rat erythrocytes, recombinant human HsMIPP1 has ability to dephosphorylate 2,3-bisphospho-D-glycerate, acute pH sensitivity of human MIPP1 offers a means to regulate hemoglobin oxygen affinity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.3
-
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
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MINP1_HUMAN
487
0
55051
Swiss-Prot
Secretory Pathway (Reliability: 5)
B2R7D2_HUMAN
487
0
55120
TrEMBL
Secretory Pathway (Reliability: 5)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
human, recombinant HsMIPP1 protein, after treatment with endoglycosidase, the protein migrates with a lower apparent size
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H89A
-
mutant of recombinant HsMIPP1 protein, 1% of the 2,3-bisphospho-D-glycerate phophatase activity of the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, human recombinant HsMIPP1 protein with a C-terminal myc-poly(His) epitope tag by using the Pichia pastoris expression system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cho, J.; King, J.S.; Qian, X.; Harwood, A.J.; Shears, S.B.
Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt
Proc. Natl. Acad. Sci. USA
105
5998-6003
2008
Dictyostelium discoideum (Q54NE6), Gallus gallus, Homo sapiens
EXTERNAL LINKS (specific for EC-Number 3.1.3.80)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
