Calculate enzyme kinetics using the Michaelis-Menten equation. Determine reaction velocity, maximum rate (Vmax), substrate concentration, and Michaelis constant (Km) for enzyme-catalyzed reactions.
Calculated Value
--
Enzyme Saturation
--
Velocity at Km
--
The Michaelis-Menten equation describes enzyme kinetics: v = (Vmax × [S]) / (Km + [S]). It shows how reaction velocity changes with substrate concentration for enzyme-catalyzed reactions.
Km is the Michaelis constant, representing the substrate concentration at which the reaction velocity is half of Vmax. Lower Km indicates higher enzyme affinity for the substrate.
Vmax can be determined by measuring reaction velocities at various substrate concentrations and fitting the data to the Michaelis-Menten equation, or by using linearization methods like Lineweaver-Burk plots.
Enzyme saturation occurs when all enzyme active sites are occupied by substrate. At saturation, increasing substrate concentration doesn't increase reaction velocity, which approaches Vmax.
The model is accurate for simple enzyme reactions with single substrates under steady-state conditions. It may not apply to complex reactions with multiple substrates or allosteric enzymes.
Common units include μM or mM for concentrations, and μmol/min or mol/s for reaction rates. Ensure all units are consistent throughout your calculations.