The enzyme could become spatially distorted, thus reducing the ability of the active site to catalyze the reaction. Tight enzyme-substrate binding will reduce the forward rate constant for the reaction. Tight binding of the enzyme to its substrate will pull the substrate out of solution, thus decreasing the driving force for the forward reaction. Tight binding of the enzyme to its substrate will result in the enzyme-transition state complex being higher in energy than with weaker binding. All of the above.