Comment on 'Computational Studies of Enzyme-Catalyzed Reactions: Where Are We in Predicting Mechanisms and in Understanding the Nature of Enzyme Catalysis'

摘要

Regarding the recent discussion between two theoretical groups on the entropic contribution to enzyme catalysis, I would like to make some comments from an experimental view-point. At issue is how much entropy and free energy reduction is brought by preorganization, i.e., bringing reactants scattered in the solution into close proximity (restricting translational motions) and optimal alignment (restricting rotational motions) in the enzyme. Here, I will not get into the issue of motional free-dom of the reactants in the enzyme-substrate complex. Rather, dom comments concern the translational and rotational motions of a solute molecule in the solution, i.e., how much motional freedom is there to be reduced through preorganization?