Enzyme Kinetics Lab

This simulator visualizes Michaelis-Menten enzyme kinetics at the molecule level: individual substrate particles diffuse through a chamber, bind a free enzyme's active site to form an ES complex, and are released as product after a randomized catalytic dwell time. A live rolling measurement of the reaction velocity is plotted alongside the theoretical V = Vmax[S]/(Km+[S]) curve, so you can watch the classic saturation kinetics emerge from thousands of individual binding events rather than just reading the formula. Adjust substrate concentration, enzyme affinity (Km), turnover rate (kcat) and enzyme count to see how each reshapes the rate curve.