Bisphosphoglycerate mutase
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2008-05-31T12:55:25Z
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{{Protbox
|Name=2,3-bisphosphoglycerate mutase
|Photo=Phosphoglycerate mutase 3PGM wpmp.png
|Caption={{{!}} align="center" border="0"
{{!}} '''Enzyme'''
{{!}} Phosphoglycerate mutase
{{!}}-
{{!}} '''PDB Code'''
{{!}} {{PDB|3PGM}}
{{!}}-
{{!}} '''Organism'''
{{!}} [[Yeast]]
{{!}}}
| HGNCid = 1093
| Symbol = BPGM
|AltSymbols =
| 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 regulation|allosteric inhibitor]] of [[hemoglobin]]. The binding of 2,3-BPG decreases hemoglobin's affinity for oxygen and facilitates the transfer of O<sub>2</sub> to tissues. BPGM plays an important role in erythrocytes, diverting up to 20% of the total [[metabolic flux|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 [[Substrate-level phosphorylation|phosphorylation]] of [[Adenosine diphosphate|ADP]] to form [[Adenosine triphosphate|ATP]]. The two-step BPGM/phosphatase pathway doesn't generate ATP and is therefore an inefficient way to arrive at G3P.
==External links==
* {{cite journal |author=Fujita T et al |title=Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro |journal=J Biochem (Tokyo) |volume=124 |issue=6 |pages=1237–44 |year=1998 |pmid=9832630 |url=http://jb.oxfordjournals.org/cgi/content/abstract/124/6/1237 }}
* {{MeshName|Bisphosphoglycerate+mutase}}
{{Mutases}}
{{Glycolysis enzymes}}
{{isomerase-stub}}
{{metabolism-stub}}
[[it:Bisfosfoglicerato mutasi]]