Bisphosphoglycerate mutase
- Bisphosphoglycerate mutase
Protbox
Name=2,3-bisphosphoglycerate mutase
Photo=Phosphoglycerate mutase 3PGM wpmp.pngCaption={! align="center" border="0"! Enzyme! Phosphoglycerate mutase!-! PDB Code!-! Organism! Yeast
HGNCid = 1093
Symbol = BPGM
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Chromosome = 7
Arm = q
Band = 31
LocusSupplementaryData = -q34
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EntrezGene = 669
OMIM = 222800
RefSeq = NM_001724
UniProt = P07738
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ECnumber = 5.4.2.4
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Bisphosphoglycerate mutase (BPGM) catalyzes the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 2,3-bisphosphoglycerate (2,3-BPG). This enzyme should not be confused with Phosphoglycerate mutase (PGM) which plays a major role in glycolysis.
While 1,3-BPG is an important intermediate in Glycolysis, 2,3-BPG is not. 2,3-BPG does have an important role in erythrocytes, acting as an allosteric inhibitor of hemoglobin. The binding of 2,3-BPG decreases hemoglobin's affinity for oxygen and facilitates the transfer of O2 to tissues. BPGM plays an important role in erythrocytes, diverting up to 20% of the total glycolytic flux in order to maintain concentrations of 2,3-BPG that are roughly equal to concentrations of hemoglobin.
Excess amounts of 2,3-BPG can re-enter the glycolytic pathway through a phosphatase catalyzed conversion to glycerate 3-phosphate (G3P). This two-step process parallels Step 7 of main glycolytic pathway in which 1,3-BPG is converted directly to G3P with the phosphorylation of ADP to form ATP. The two-step BPGM/phosphatase pathway doesn't generate ATP and is therefore an inefficient way to arrive at G3P.
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Look at other dictionaries:
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