The development of enzyme mimetic catalysts as well as the analysis of the catalytic effects of such catalysts has been a major challenge for synthetic chemists. One of the impressive examples of artificial catalysts has been the development of a highly charged host compound that provides a significant acceleration to the hydrolysis of orthoformates and other systems. However, the origin of the catalytic effect has not been quantified, and its origin remains somewhat. unclear. The understanding of the corresponding supramolecular catalysis has thus become a major challenge, both in terms of Computational. modeling and in terms of the analysis of the corresponding acid-catalyzed reaction. Here we present a computer simulation study and kinetic analyses that reproduce the experimentally, observed catalytic effect, establishing that this effect is due to electrostatic stabilization of the positively Charged transition state (relative to the uncharged bound complex). Our study illustrates the crucial need for careful analysis of the complex kinetics of the catalytic effect and the host system, as well as the need for computational Modeling in analyzing the catalytic effect and the potential design of better catalysts.. Finally, our finding of the large stabilization Of the bound H3O+ points out the very low "local pH" inside the host system even when the solvent is kept at a high pH.