Phosphoglycerate Mutase: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 2: | Line 2: | ||
== Background == | == Background == | ||
[[Glycolysis]] is a 10-step process that invests energy in the initial stages only to recover greater amounts of energy in the final steps. Every step in this metabolic pathway is essential to the ultimate production of energy. Every step is catalyzed by one or more enzymes that enhance the rate of the given reaction. '''Phosphoglycerate mutase''' (PGM) is the specific homotetramer enzyme that catalyzes step 8 of glycolysis transfering the phosphate from 3-phosphoglyceric acid to the second carbon to form 2-phosphoglyceric acid, having the Protein Data Bank ID [[1qhf]]<ref>PMID:10531478</ref>. PGM is found in organisms from yeast to humans because it plays a significant role in glycolysis, which is a highly conserved process across many taxa. A deficiency of this enzyme causes CNS symptoms, muscle weakness, cramps and fatigue with exercise. '''2,3-bisphosphoglycerate-independent phosphoglycerate mutase''' (BIPGM) is found in archaea and eubacteria. It catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | [[Glycolysis]] is a 10-step process that invests energy in the initial stages only to recover greater amounts of energy in the final steps. Every step in this metabolic pathway is essential to the ultimate production of energy. Every step is catalyzed by one or more enzymes that enhance the rate of the given reaction. '''Phosphoglycerate mutase''' (PGM) is the specific homotetramer enzyme that catalyzes step 8 of glycolysis transfering the phosphate from 3-phosphoglyceric acid (3PG) to the second carbon to form 2-phosphoglyceric acid (2PG), having the Protein Data Bank ID [[1qhf]]<ref>PMID:10531478</ref>. PGM is found in organisms from yeast to humans because it plays a significant role in glycolysis, which is a highly conserved process across many taxa. A deficiency of this enzyme causes CNS symptoms, muscle weakness, cramps and fatigue with exercise. '''2,3-bisphosphoglycerate-independent phosphoglycerate mutase''' (BIPGM) is found in archaea and eubacteria. It catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | ||
<ref>http://disability.ucdavis.edu/disease_deatails.php?id=45</ref> | <ref>http://disability.ucdavis.edu/disease_deatails.php?id=45</ref> | ||
| Line 71: | Line 71: | ||
**[[4emb]] – PGM – ''Borrelia burgdorferi''<br /> | **[[4emb]] – PGM – ''Borrelia burgdorferi''<br /> | ||
**[[4eo9]] – PGM – ''Mycobacterium leprae''<br /> | **[[4eo9]] – PGM – ''Mycobacterium leprae''<br /> | ||
**[[4my4]] – | **[[4my4]] – SaPGM – ''Staphylococcus aureus''<br /> | ||
**[[2a9j]], [[2h4x]], [[2h52]] – hPGM + | **[[4nwj]] – SaPGM + 3PG<br /> | ||
**[[2f90]] - hPGM + | **[[4nwx]], [[4qax]] – SaPGM + 2PG<br /> | ||
**[[2a9j]], [[2h4x]], [[2h52]] – hPGM + 3PG<br /> | |||
**[[2f90]] - hPGM + 3PG + AlF4<br /> | |||
**[[2h4z]], [[2hhj]] – hPGM + 2,3-BGP<br /> | **[[2h4z]], [[2hhj]] – hPGM + 2,3-BGP<br /> | ||
**[[1ejj]] - GsPGM + | **[[1ejj]] - GsPGM + 3PG – ''Geobacillus stearothermophilus''<br /> | ||
**[[1eqj]] - GsPGM + | **[[1eqj]] - GsPGM + 2PG<br /> | ||
**[[3idd]], [[3kd8]] – TaBIPGM – ''Thermoplasma acidophilum''<br /> | **[[3idd]], [[3kd8]] – TaBIPGM – ''Thermoplasma acidophilum''<br /> | ||
**[[3nvl]] – BIPGM - ''Trypanosoma brucei''<br /> | **[[3nvl]] – BIPGM - ''Trypanosoma brucei''<br /> | ||