What is Michaelis menten hypothesis

The Michaelis-Menten hypothesis describes the kinetics of enzyme-catalyzed reactions. It proposes that an enzyme (E) reversibly binds to its substrate (S) to form an enzyme-substrate complex (ES), which then breaks down to form product (P) and free enzyme (E).

The key assumptions are:

1. The formation of the ES complex is a rapid equilibrium.
2. The breakdown of ES to form product is the rate-limiting step.
3. The concentration of ES is constant over time (steady-state assumption).

This leads to the Michaelis-Menten equation:
v = (Vmax * [S]) / (Km + [S])

Where:

• v is the initial reaction velocity.
• Vmax is the maximum reaction velocity when the enzyme is saturated with substrate.
• [S] is the substrate concentration.
• Km is the Michaelis constant, representing the substrate concentration at which the reaction velocity is half of Vmax.