BCHM 3114 Study Guide - Comprehensive Final Exam Guide - Glycolysis, Adenosine Triphosphate, Oxygen
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E + s e*s e * p e +p: define the active site of an enzyme and describe how it determines an enzyme"s specificity. Enzymes are highly specific for their substrates due to active site complementarity with the substrate: explain the basis for the observation that enzyme-catalyzed reactions are saturable. Activation energy= energy needed to carry out the reaction (g) The point of highest energy is the transition state: draw a reaction coordinate diagram of a simple reaction (i. e. , with reactant(s) and product(s) but no intermediates). Label g, g , and the position of the transition state. Indicate whether the reaction is spontaneous, nonspontaneous or at equilibrium: explain the relationship between the reaction rate and the height of the free energy activation barrier ( g ). Enzymes lower the transition state and activation energy: explain what is meant by the steady state assumption in enzyme kinetics.
