Enzyme Inhibition Kinetics: Competitive vs Non-Competitive (2D)

This 2D companion to the 3D "Enzyme Kinetics Simulator" trades the molecule-by-molecule reaction vessel for the quantitative view a biochemist actually reads a kinetics dataset with. The same active-site chemistry — substrate binding, complex formation, product release — is driven here by the real modified Michaelis-Menten rate law, extended to cover all four classical inhibition mechanisms: competitive (inhibitor competes with substrate for the free enzyme), uncompetitive (inhibitor binds only the enzyme-substrate complex), noncompetitive (inhibitor binds free enzyme and complex with equal affinity) and mixed (independent affinities for each). Three panels update together from the same five parameters — Vmax, Km, inhibitor type, [I], Ki and Ki′: a saturation curve overlaying the inhibited and uninhibited v-vs-[S] curves, a Lineweaver-Burk double-reciprocal plot that makes the textbook diagnostic signature directly visible (competitive inhibition changes the slope but not the y-intercept; pure noncompetitive inhibition changes the y-intercept but not the x-intercept), and a substrate-depletion time course that numerically integrates dS/dt = -v(S) with 4th-order Runge-Kutta so you can watch a real reaction actually run to completion rather than only see its instantaneous rate.