Christopher Vachon Sandbox: Difference between revisions
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One exception includes the PGM enzyme of yeast which is a <scene name='Christopher_Vachon_Sandbox/Tetrameric/1'>homotetramer</scene> of mass 110,000 kDa. <ref name="winn" /> Though the quaternary structure is the same in terms of the active site, several variations exist, called isozymes, which depend on the tissue in which the enzyme is active. Mm-type, mb-type, and bb-type are isozymes that catalyze glycolysis in smooth muscle, cardiac and skeletal muscle, and the remaining tissues, respectively.<ref>"Phosphoglycerate mutase -." Wikipedia, the free encyclopedia. Web. 27 Feb. 2010. <http://en.wikipedia.org/wiki/Phosphoglycerate_mutase>.</ref> {{STRUCTURE_1qhf | PDB=1qhf | SCENE= }} | One exception includes the PGM enzyme of yeast which is a <scene name='Christopher_Vachon_Sandbox/Tetrameric/1'>homotetramer</scene> of mass 110,000 kDa. <ref name="winn" /> Though the quaternary structure is the same in terms of the active site, several variations exist, called isozymes, which depend on the tissue in which the enzyme is active. Mm-type, mb-type, and bb-type are isozymes that catalyze glycolysis in smooth muscle, cardiac and skeletal muscle, and the remaining tissues, respectively.<ref>"Phosphoglycerate mutase -." Wikipedia, the free encyclopedia. Web. 27 Feb. 2010. <http://en.wikipedia.org/wiki/Phosphoglycerate_mutase>.</ref> {{STRUCTURE_1qhf | PDB=1qhf | SCENE= }} | ||
== Reaction and Mechanism == | == Reaction and Mechanism == | ||
PGM is an integral step in the process of glycolysis. Since this enzyme is a mutase, it will catalyze the transfer of a functional group from one position to another on a given substrate makin this an isomerization reaction. It is responsible for the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG), having 2,3-bisphosphoglycerate as an intermediate. <ref name="voet">Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref> With a Gibbs free energy of about 1.1 KJ/mol, this reaction is nearly energetically neutral. Despite this, it is absolutely necessary in order to generate the proper molecule needed to continue in the glycolytic pathway. | PGM is an integral step in the process of glycolysis. Since this enzyme is a mutase, it will catalyze the transfer of a functional group from one position to another on a given substrate makin this an isomerization reaction. It is responsible for the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG), having 2,3-bisphosphoglycerate as an intermediate. <ref name="voet">Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. Print.</ref> With a Gibbs free energy of about 1.1 KJ/mol, this reaction is nearly energetically neutral. Despite this, it is absolutely necessary in order to generate the proper molecule needed to continue in the glycolytic pathway. | ||
It is important to note that the phosphate group that is placed on C2 is not the same phosphate group that was initially on C3. | It is important to note that the phosphate group that is placed on C2 is not the same phosphate group that was initially on C3. | ||