Bisphosphoglycerate Mutase (BPGM)
2,3-Bisphosphoglycerate Mutase; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; BPG-dependent PGAM
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Bisphosphoglycerate mutase (BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolitic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent.
Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes and placental cells. In glycolysis, converting 1,3-BPG to 2,3-BPG would be very inefficient, as it just adds another unnecessary step.
Organism species: Homo sapiens (Human)
- Recombinant protein RPD716Hu01 Recombinant Bisphosphoglycerate Mutase (BPGM) In Stock
- Polyclonal antibody PAD716Hu01 Polyclonal Antibody to Bisphosphoglycerate Mutase (BPGM) In Stock
- Sandwich ELISA SED716Hu ELISA Kit for Bisphosphoglycerate Mutase (BPGM) In Stock
Organism species: Mus musculus (Mouse)
- Recombinant protein RPD716Mu01 Recombinant Bisphosphoglycerate Mutase (BPGM) In Stock
- Polyclonal antibody PAD716Mu01 Polyclonal Antibody to Bisphosphoglycerate Mutase (BPGM) In Stock
- Sandwich ELISA SED716Mu ELISA Kit for Bisphosphoglycerate Mutase (BPGM) In Stock
Organism species: Rattus norvegicus (Rat)
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