The type of interactions occurring between two molecules in an enzymatic reaction are primarily based on non-covalent interactions such as hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions. The enzyme's active site specifically binds to the substrate, facilitating the conversion of substrate into product. This interaction is characterized by a high degree of specificity, allowing enzymes to catalyze only particular reactions, thereby enhancing reaction rates. These interactions are crucial for the efficient functioning of biological processes, enabling enzymes to lower activation energy and increase the speed of chemical reactions within the cell.