In 1913, scientists Michael and Menten expressed the theory about the mechanism of action of enzymes called Michaelis-Menten theory. This doctrine is similar to the doctrine of lock and key. The doctrine is discussed.
An enzyme is a type of protein made up of numerous amino acids. The site of apoenzyme where the substrate binds and causes the reaction is called the active site. Each enzyme has one or more active sites or reaction centers. The substrate binds to the enzyme’s active site or reaction center to form an enzyme-substrate complex. Enzymes dissociate after product formation. The rate of enzyme reaction is related to the concentration of substrate. As the concentration of substrate increases, the rate of enzyme action increases. The Michaelis constant (Km) of the reaction is called the Michaelis constant (Km) of the reaction half the maximum speed due to increase in substrate concentration. The Michaelis constant is a special feature of enzymes. The rate of reaction is determined by the value of Km.