v = Vmax·[S] / (K_M + [S]). Derived from E + S ⇌ ES → E + P under the steady-state approximation (Briggs-Haldane 1925). Describes hyperbolic initial-rate curves of non-allosteric enzymes.
Michaelis-Menten kinetics
Related concepts
- Enzyme
- Chemical equilibrium
- Rate-determining step
- Turnover number k_cat
- Michaelis constant K_M
- Lineweaver-Burk (double-reciprocal) plot
- Competitive inhibition
- Non-competitive inhibition
- Uncompetitive inhibition
- GPCR signaling (Lefkowitz-Kobilka)
- Myosin cross-bridge cycle (Huxley 1957)
- Hexokinase isozymes (Crane 1955)
- Transamination (Schlenk 1942)
- Monod growth (1949)