🧪 Michaelis-Menten & Competitive Inhibition

This simulator models real Michaelis-Menten enzyme kinetics. A fixed population of enzyme molecules is exposed to a substrate concentration [S] that you control; the reaction rate v follows v = Vmax·[S]/(Km + [S]), the same equation that describes real enzyme-catalyzed reactions saturating at high substrate levels. Toggle on a competitive inhibitor to see it raise the apparent Km (Km,app = Km·(1 + [I]/Ki)) while leaving the true Vmax untouched — the hallmark of competitive inhibition. Individual enzyme molecules in the reaction chamber switch between free, substrate-bound and inhibitor-bound states at rates drawn from the same equilibrium fractions the formula predicts, so the animation and the math stay consistent. Record measurements (or run an automatic sweep across [S]) to build a live Lineweaver-Burk double-reciprocal plot and read Km and Vmax directly off its intercepts, just as in a real kinetics assay.