 |
One of the ways biochemists characterize enzymes is to study the rates of enzyme-catalyzed reactions, a field known as enzyme kinetics. The study of enzyme kinetics provides researchers with clues as to how enzymes work. In 1913, Leonor Michaelis and Maud Menten derived a rate law that governs enzyme kinetics. |
Michaelis-Menten enzyme kinetics can be modeled by the rational function,
where V represents the reaction velocity, Vmax represents the maximum reaction velocity, Km represents the Michaelis-Menten constant, and [S] represents the substrate concentration. The velocity of the reaction, V,is dependent on the substrate concentration, [S].
Note of caution
This equation assumes that during the reaction the concentration of the enzyme-substrate complex remains constant and is lower than the concentrations of unbound substrate. These conditions are known as steady-state. |
|