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Bisphosphoglycerate mutase : ウィキペディア英語版
Bisphosphoglycerate mutase

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.
== Tissue distribution ==

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. Since the main role of 2,3-BPG is to shift the equilibrium of hemoglobin toward the deoxy-state, its production is really only useful in the cells which contain hemoglobin- erythrocytes and placental cells.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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