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I am currently in the process of studying enzyme catalysis and am struggling to get to grips with this concept. As far as I understand, the propinquity effect allows substrates to bind with enzymes in the conformation which would facilitate the reaction, thus increasing the reaction rate. Could someone expand on the why and/or how enzymes are able to do this? What specific reactions benefit from this the most?

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how: an enzyme is able to effectively make a reaction intramolecular by binding the reactants in the correct conformation in close proximity within the active site this can speed up the rate of a reaction dramatically, intramolecular rates avoid diffusion control and have prearranged conformations which is far more efficient than typical intermolecular reactions, why: enzymes are outrageous, evolution has pushed them, through trial and error, towards optimal configurations that, almost magically, provide ideal conditions for a reaction to occur

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