After an enzyme binds to its substrate, it stabilizes the transition state by reducing activation energy and hence increases the rate of a reaction by providing an alternative chemical pathway for the reaction. Enzymes have rather flexible structures and the active site of an enzyme can be modified as the substrate interacts with the enzyme. The initial interaction between enzyme and substrate is relatively weak, but this weak interaction can rapidly induce structural rearrangements in the enzyme that strengthen binding. Therefore, the older theory about "the lock and key" model where a particular domain on the surface of the enzyme is structured to have a precise complementary fit to the substrate is not always a requirement for binding. Enzyme activity can be affected by various environmental parameters such as pH, temperature, pressure, ionic strength; by the addition of organic solvents or various kosmotropes and chaotropes which may stabilize or destabilize enzymes in
After an enzyme binds to its substrate, it stabilizes the transition state by reducing activation energy and hence increases the rate of a reaction by providing an alternative chemical pathway for the reaction. Enzymes have rather flexible structures and the active site of an enzyme can be modified as the substrate interacts with the enzyme. The initial interaction between enzyme and substrate is relatively weak, but this weak interaction can rapidly induce structural rearrangements in the enzyme that strengthen binding. Therefore, the older theory about "the lock and key" model where a particular domain on the surface of the enzyme is structured to have a precise complementary fit to the substrate is not always a requirement for binding. Enzyme activity can be affected by various environmental parameters such as pH, temperature, pressure, ionic strength; by the addition of organic solvents or various kosmotropes and chaotropes which may stabilize or destabilize enzymes in