Michaelis–Menten Enzyme Kinetics: Derivation and Interpretation
Physical Chemistry · Kinetics Michaelis–Menten Enzyme Kinetics: Derivation and Interpretation A steady-state derivation applied to a biological catalyst, giving two constants whose meanings are constantly confused. BSc & MSc · Physical Chemistry · Concept The short answer: Apply the steady-state approximation to the enzyme–substrate complex and the rate becomes v = Vmax[S]/(KM + [S]). KM is the substrate concentration at half maximal rate and indicates how tightly the substrate binds; Vmax reflects how fast the enzyme turns over once saturated. The mechanism E + S ⇌ ES (k1 forward, k−1 reverse) ES → E + P (k2) The enzyme…