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).
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The enzyme appears in viruses and cellular organisms
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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).
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
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
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
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
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 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
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 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 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
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
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
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
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
expressed in Escherichia coli, human recombinant HsMIPP1 protein with a C-terminal myc-poly(His) epitope tag by using the Pichia pastoris expression system