Christopher Vachon Sandbox: Difference between revisions
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==The Catalytic Ability of Phosphoglycerate Mutase=={{STRUCTURE_1qhf | PDB=1qhf | SCENE= }} | ==The Catalytic Ability of Phosphoglycerate Mutase=={{STRUCTURE_1qhf | PDB=1qhf | SCENE= }} | ||
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 is the specific enzyme that catalyzes step 8 of glycolysis[[1qhf]]<ref>PMID:10531478</ref>. Phosphoglycerate mutase (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. | 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 is the specific enzyme that catalyzes step 8 of glycolysis, having the Protein Data Bank ID[[1qhf]]<ref>PMID:10531478</ref>. Phosphoglycerate mutase (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. | ||
In terms of the <scene name='Christopher_Vachon_Sandbox/Secondary_structures/1'>Secondary Structures</scene>, this protein is classified as an alpha/beta protein. Further, the fold is classified as “phosphoglycerate mutase-like”, having 3 main layers of alpha/beta/alpha. PGM contains a mixed beta sheet of 6 strands, with strand 5 existing as an anti-parallel strand to the rest. The quaternary structure usually is comprised of two identical subunits, thus this enzyme can be classified as a homodimer. The dimers have a relative molecular mass of 56,000-60,000 kDa. <ref name="winn">S., Winn I., Fothergill A. L., Harkins N. R., and Watson C. H. "Structure and Activity of Phosphoglycerate Mutase." Sciences 293.1063 (1981): 121-30. Print.</ref> | In terms of the <scene name='Christopher_Vachon_Sandbox/Secondary_structures/1'>Secondary Structures</scene>, this protein is classified as an alpha/beta protein. Further, the fold is classified as “phosphoglycerate mutase-like”, having 3 main layers of alpha/beta/alpha. PGM contains a mixed beta sheet of 6 strands, with strand 5 existing as an anti-parallel strand to the rest. The quaternary structure usually is comprised of two identical subunits, thus this enzyme can be classified as a homodimer. The dimers have a relative molecular mass of 56,000-60,000 kDa. <ref name="winn">S., Winn I., Fothergill A. L., Harkins N. R., and Watson C. H. "Structure and Activity of Phosphoglycerate Mutase." Sciences 293.1063 (1981): 121-30. Print.</ref> | ||
