Enzyme rates and kinetics are key components used by biochemists to understand how enzymes function. However, students often find it difficult to understand how these experiments are performed and how they reflect enzyme behavior in solution. The microscopic behaviors which compose K_M, V_max, and other kinetic parameters are not easy to see, hindering clear incorporation of kinetics into students' biochemical knowledge. We describe a set of in-class activities where students act as enzymes in order to clarify the behavior of enzymes in solution and to develop a more robust understanding of how kinetics describe this behavior. In the first demonstration, students observe how the rate of candy unwrapping changes over time in a closed system showing how products can slow the progress of an enzyme reaction. In the second demonstration, students observe how substrate concentration and the rate of enzyme reactions are linked and eventually saturate. A final aspect of this lesson helps students learn how to fit their own data to calculate the kinetic values V_max and K_M. Extensions of this activity to enzyme inhibition and active site structure are also described. Students felt more confident in their understanding of enzyme kinetics and action after performing these activities.