BPGM Protein, Human (His)
BPGM Protein, Human (His) expresses in E. coliwith a His tag. Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin.
- Species: Human
- Source: E. coli
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Biological Activity
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Product Properties
- Documentation
- References
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Biological Activity
BPGM Protein, Human (His) expresses in E. coliwith a His tag. Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin[1].
Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specifictri-functional enzyme, catalyzing a series of intermolecular phosphoryl group transfer reactions. The main activity of BPGM is synthase, converting 1,3-bisphosphoglycerate(1,3-BPG) to 2,3-bisphosphoglycerate (2,3-BPG). The second activity is mutase, catalyzingthe inter-conversion between 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). The third activity is phosphatase, hydrolyzing the 2,3-BPG to 3-PGA or 2-PGA and a phosphate. BPGM is found in erythrocytes and placental cells, and itregulates the level of 2,3-BPG[2].
Technical Parameters
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Species Human
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Source E. coli
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Tag C-6*His
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Accession
P07738 (S2-K259)
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Molecular Construction
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N-term
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BPGM (S2-K259)
Accession # P07738 -
6*His
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C-term
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Protein Length
Extracellular Domain
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Synonyms
BPGM; DPGM; Bisphosphoglycerate Mutase; Testis Secretory Sperm-Binding Protein Li 202a; 2,3-Bisphosphoglycerate Mutase, Erythrocyte; Erythrocyte 2,3-Bisphosphoglycerate Mutase; 2,3-Bisphosphoglycerate Synthase; 2,3-Bisphosphoglycerate Mutase; 2,3-Diphosph
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AA Sequence
SKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK
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Predicted Molecular Mass
31 kDa
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Molecular Weight
Approximately 30 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Documentation
References
[1]. Wang Y, et al. Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. J Biol Chem. 2006;281(51):39642-39648. [Content Brief]
[2]. Chu WT, et al. Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation. Phys Chem Chem Phys. 2014;16(9):3946-3954. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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