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Department
Biology
Course
BIOL 241
Professor
William Huddleston
Semester
Winter

Description
ALL Reactions Require Activation Energy - After you have reached the top, that’s the transition state. Glucose + ATP -> glucose-6-Pi +H2O - If you add a catalyst, the Ea goes down Delta G does not change How do enzymes reduce the EA required? Enzyme structure determines function - An enzyme is typically a large molecule, made up of one or more polypeptide chains, folded into a very specific 3D conformation (shape) Every enzyme has an active site - A region that interacts with a specific substrate (or specific substrates) - When a substrate enters the active site, they bind, forming temporary bonds, and an enzyme- substrate complex ( E + S E*S) The ES complex changes conformation creating an induced fit - The new shape fits the transition state where the bonds in the substrate break and the bonds in the products form By forcing the substrate in to the transition state, the enzyme reduces the need for as much Ea The products are then released and the enzyme changes back to its original conformation (E + S ES EP E + P) 1. Hexokinase binds to Glucose E+ S1 ES1 2. Induced Fit Stresses Substrate 3. Hexokinase binds to ATP ES1 + S2 EP1P2 5. Products are released and enzyme returns to original conformation EP1P2 -> E + P1 + P2 Why don’t our cells manipulate the concentration of ADP and Pi to make the formation of ATP spontaneous? ADP + Pi -> ATP delta G =52kj/mol ATP/((ADP)(Pi)) =1 Too much would be required to do that. We would need a billion molar ADP to get to -1kj/mol Remember, delta G must be negative for a reaction to happen in a cell, even if the same reaction has a Delta G(degree) that is positive. Coupled Reactions -the reaction which produces glucose-6-Pi looks like two reactions added together: 1.Glucose is phosphorylated 2.ATP hydroly
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