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Literature summary extracted from
- Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt (2008), Proc. Natl. Acad. Sci. USA, 105, 5998-6003.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.62 | expressed in Pichia pastoris | Homo sapiens |
| 3.1.3.80 | electroporation of Ax2 cells with the plasmid pJSK166, generated by cloning the full coding sequence into the extrachromosomal expression vector pRHI8 | Dictyostelium discoideum |
| 3.1.3.80 | expressed in Escherichia coli | Gallus gallus |
| 3.1.3.80 | expressed in Escherichia coli, human recombinant HsMIPP1 protein with a C-terminal myc-poly(His) epitope tag by using the Pichia pastoris expression system | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.3.62 | H89A | catalytically compromised mutant of MIPP1 that shows only 1% of the 2,3-diphosphoglycerate phosphatase activity of the wild type enzyme | Homo sapiens |
| 3.1.3.80 | H89A | mutant of recombinant HsMIPP1 protein, 1% of the 2,3-bisphospho-D-glycerate phophatase activity of the wild-type enzyme | Homo sapiens |
| 3.1.3.80 | T27G | mutant of recombinant chicken MIPP1 protein, more than 95% lower activity than wild-type enzyme | Gallus gallus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.62 | 0.61 | - |
2,3-bisphosphoglycerate | recombinant enzyme, at 37°C | Homo sapiens |  |
| 3.1.3.80 | 0.61 | - |
2,3-bisphospho-D-glycerate | phosphatase activity of deglycosylated human HsMIPP1 protein | Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.62 | plasma membrane | - |
Homo sapiens | 5886 | - |
| 3.1.3.62 | plasma membrane | - |
Rattus norvegicus | 5886 | - |
| 3.1.3.80 | plasma membrane | - |
Homo sapiens | 5886 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.62 | 55000 | - |
deglycosylated recombinant protein, SDS-PAGE | Homo sapiens |
| 3.1.3.62 | 55000 | - |
deglycosylated recombinant protein, SDS-PAGE | Rattus norvegicus |
| 3.1.3.62 | 70000 | - |
glycosylated recombinant protein, SDS-PAGE | Homo sapiens |
| 3.1.3.62 | 70000 | - |
glycosylated recombinant protein, SDS-PAGE | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | Homo sapiens | 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-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | Gallus gallus | 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, physiologically relevant regulation of cellular 2,3-bisphospho-D-glycerate content | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | Dictyostelium discoideum | additional bisphosphoglycerate phosphatase identified, 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, 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-phospho-D-glycerate + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.62 | Dictyostelium discoideum | - |
- |
- |
| 3.1.3.62 | Homo sapiens | - |
- |
- |
| 3.1.3.62 | Rattus norvegicus | - |
- |
- |
| 3.1.3.80 | Dictyostelium discoideum | Q54NE6 | Ax2 wild-type background | - |
| 3.1.3.80 | Gallus gallus | - |
- |
- |
| 3.1.3.80 | Homo sapiens | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.3.62 | glycoprotein | - |
Homo sapiens |
| 3.1.3.62 | glycoprotein | - |
Rattus norvegicus |
| 3.1.3.80 | glycoprotein | human, recombinant HsMIPP1 protein, after treatment with endoglycosidase, the protein migrates with a lower apparent size | Homo sapiens |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.62 | Ni-Sepharose column chromatography | Homo sapiens |
| 3.1.3.62 | Ni-Sepharose column chromatography | Rattus norvegicus |
| 3.1.3.80 | gel filtration | Gallus gallus |
| 3.1.3.80 | gel filtration | Homo sapiens |
| 3.1.3.80 | gel filtration | Dictyostelium discoideum |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.3.62 | erythrocyte | - |
Homo sapiens | - |
| 3.1.3.62 | erythrocyte | - |
Rattus norvegicus | - |
| 3.1.3.80 | erythrocyte | - |
Gallus gallus | - |
| 3.1.3.80 | erythrocyte | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.62 | 0.009 | - |
using 2,3-bisphosphoglycerate as substrate, at 37°C | Homo sapiens |
| 3.1.3.80 | additional information | - |
identification of a second enzyme component of the Rapoport-Luebering shunt, separate 2,3-bisphosphoglycerate phosphatase activity, catalyzed by an evolutionarily conserved multiple inositol polyphosphate phosphatase (MIPP1), considered as an important regulatory system with several roles in cell physiology, recombinant chicken MIPP1 can actively hydrolyze both 2,3-bisphospho-D-glycerate and inositol phosphates, enzyme can contribute to regulating hemoglobin oxygen affinity, single mutant version of chicken MIPP1 protein shows more than 95% lower activities indicating that a single active site is involved, specific activity of avian MIPP1 protein toward 2,3-bisphospho-D-glycerate is 50fold greater than that of human MIPP1 protein | Gallus gallus |
| 3.1.3.80 | 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 | Homo sapiens |
| 3.1.3.80 | additional information | - |
mechanism to link the turnover of phosphorylated inositol derivatives with changes in glycolytic flux, identification of a second enzyme component of the Rapoport-Luebering shunt, separate 2,3-bisphosphoglycerate phosphatase activity, 2,3-bisphospho-D-glycerate measured by coupling its hydrolysis to NADH oxidation, catalyzed by an evolutionarily conserved multiple inositol polyphosphate phosphatase (MIPP1), additional catalytic reaction can be considered as an important regulatory system with several roles in cell physiology | Dictyostelium discoideum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.62 | 2,3-bisphosphoglycerate + H2O | - |
Homo sapiens | 2-phosphoglycerate + phosphate | - |
? | |
| 3.1.3.62 | 2,3-bisphosphoglycerate + H2O | - |
Rattus norvegicus | 2-phosphoglycerate + phosphate | - |
? | |
| 3.1.3.62 | 2,3-bisphosphoglycerate + H2O | - |
Dictyostelium discoideum | 2-phosphoglycerate + phosphate | - |
? | |
| 3.1.3.62 | inositol 1,3,4,5,6-pentakisphosphate + H2O | - |
Homo sapiens | inositol 1,4,5,6-tetrakisphosphate + phosphate | - |
? | |
| 3.1.3.62 | inositol 1,3,4,5,6-pentakisphosphate + H2O | - |
Rattus norvegicus | inositol 1,4,5,6-tetrakisphosphate + phosphate | - |
? | |
| 3.1.3.62 | inositol 1,3,4,5,6-pentakisphosphate + H2O | - |
Dictyostelium discoideum | inositol 1,4,5,6-tetrakisphosphate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | 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 | Homo sapiens | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, physiologically relevant regulation of cellular 2,3-bisphospho-D-glycerate content | Gallus gallus | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | additional bisphosphoglycerate phosphatase identified, 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, 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 | Dictyostelium discoideum | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | 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 | Homo sapiens | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | additional bisphosphoglycerate phosphatase identified, 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, glycolytic pathway can bypass the formation of 3-phospho-D-glycerate, biological significance of the Rapoport-Luebering shunt | Gallus gallus | 2-phospho-D-glycerate + phosphate | - |
? | |
| 3.1.3.80 | 2,3-bisphospho-D-glycerate + H2O | additional bisphosphoglycerate phosphatase identified, 2-phospho-D-glycerate is formed from hydrolysis of 2,3-bisphospho-D-glycerate, not by mutase activity of 3-phospho-D-glycerate, glycolytic pathway can bypass the formation of 3-phospho-D-glycerate, biological significance of the Rapoport-Luebering shunt | Dictyostelium discoideum | 2-phospho-D-glycerate + phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.62 | MIPP | - |
Homo sapiens |
| 3.1.3.62 | MIPP | - |
Rattus norvegicus |
| 3.1.3.62 | MIPP | - |
Dictyostelium discoideum |
| 3.1.3.62 | multiple inositol polyphosphate phosphatase | - |
Homo sapiens |
| 3.1.3.62 | multiple inositol polyphosphate phosphatase | - |
Rattus norvegicus |
| 3.1.3.62 | multiple inositol polyphosphate phosphatase | - |
Dictyostelium discoideum |
| 3.1.3.80 | DdMipp1 | - |
Dictyostelium discoideum |
| 3.1.3.80 | HsMIPP1 protein | - |
Homo sapiens |
| 3.1.3.80 | MIPP1 protein | - |
Gallus gallus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.80 | 37 | - |
recombinant human HsMIPP1 protein | Homo sapiens |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.80 | 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 | Homo sapiens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.62 | 4 | 37 | MIPP1 is active at 4°C, albeit considerably less active than at 37°C | Homo sapiens |
| 3.1.3.62 | 4 | 37 | MIPP1 is active at 4°C, albeit considerably less active than at 37°C | Rattus norvegicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.80 | 7 | - |
recombinant human HsMIPP1 protein | Homo sapiens |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.80 | 5 | 7.3 | recombinant human HsMIPP1 protein, about 80% of maximal activity at pH 5, about 50% of maximal activity at pH 7.3 | Homo sapiens |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.62 | 7 | 7.4 | MIPP1 activity decreases 50% when pH rises from 7.0 to 7.4 | Homo sapiens |
| 3.1.3.62 | 7 | 7.4 | MIPP1 activity decreases 50% when pH rises from 7.0 to 7.4 | Rattus norvegicus |
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