User:Sydney Park: Difference between revisions

In preparation for the final step of glycolysis, Enolase is used as a catalyst to turn 2-phosphoglycerate (2-PGA) into phosphoenolpyruvate (PEP). It dehydrates the alcohol by removing a water molecule and simultaneously making a double bond between the two carbons not directly connected to the hydroxyl group. This step makes the compound relatively unstable, but also gives energy in order for the final step to occur. Enolase is also that catalyst in the reverse reaction to make PEP into 2-PGA again. 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.