Enolase: Difference between revisions

[[Image:1one.png|left|250px|thumb|Crystal Structure of Enolase, [[1one]]]]<scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> is an enzyme that catalyzes a reaction of glycolysis.  {{STRUCTURE_1one|  PDB=1one  | SIZE=400| SCENE=Enolase/Enolase/1 |right|CAPTION=Yeast enolase complex with phosphoenolpyruvate and phosphoglycerate, [[1one]] }}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>. As with the reaction below, Enolase must have a divalent metal cation present to activate or deactivate the enzyme. The best cofactor would be Mg2+, but many, including Zn2+, Mn2+ and Co2+ can be used. The metal ion works by binding to the enzyme at the active site and producing a conformational change. This makes it possible for the substrate (2-PGA) to bind at the Enolase active site. Once this happens, a second metal ion comes in and binds to the enzyme to activate the Enolase catalytic ability.