Allen sandbox 1: Difference between revisions

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Justin Allen

Revision as of 00:18, 4 April 2011 view source Justin Allen (talk \| contribs) 26 edits No edit summary ← Older edit		Revision as of 00:24, 4 April 2011 view source Justin Allen (talk \| contribs) 26 edits No edit summary Newer edit →
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	{{STRUCTURE_1one \| PDB=1one \| SCENE= }}		{{STRUCTURE_1one \| PDB=1one \| SCENE= }}

	<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of ~~glycolysis. Glycolysis converts glucose~~ into ~~two 3-carbon molecules called pyruvate. The energy released during~~ glycolysis ~~is used to make ATP~~.<ref>{{textbook \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=~~487~~\|}}</ref> ~~Enolase~~ is used to ~~convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction~~.<ref>{{textbook \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=~~500~~\|}}</ref>. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>.		<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes the reversible dehydration reaction of 2-phosphoglycerate (2PG) into Phosphophenolglycerate (PEP) in the 9th reactiion of glycolysis.<ref>{{textbook \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=500\|}}</ref>. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.<ref>{{textbook \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=487\|}}</ref>. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis, especially for those enzymes involved in glycolysis <ref>{{journal}}</ref>.