EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
  3.1.3.80 | -999 |
- |
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 |
694894 |
| 3.1.3.80 | -999 |
- |
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 |
694894 |
| 3.1.3.80 | -999 |
- |
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 |
694894 |
