🧪 Chemistry Biochemistry Simulation

This simulation puts Michaelis-Menten enzyme kinetics inside a living 3D reaction chamber. Substrate molecules diffuse freely until they encounter a free active site on one of the enzyme molecules, bind briefly to form an enzyme-substrate complex, and are released as product after a turnover delay — the same E + S ⇌ ES → E + P mechanism that governs real catalysis inside every living cell, from digestive enzymes to the machinery of metabolism. Adjust substrate concentration, enzyme count, binding affinity (K_m) and turnover rate (k_cat) to see the classic Michaelis-Menten rate curve build itself in real time, or switch on a competitive inhibitor to watch it raise the apparent K_m while V_max stays fixed — the textbook kinetic fingerprint biochemists use to classify how a drug or toxin blocks an enzyme.