The Lock and Key hypothesis

The hypothesis proposed that the active site and substrate are exactly complementary. An enzyme is a large globular protein with a specific three-dimensional shape. It has a groove called the active site containing amino acid side chains that complementary to the substrate. In the lock-and-key hypothesis, the shape of the substrate (key) fits into the rigid active site of the enzyme (lock) forming an enzyme-substrate complex. Reaction takes place and products are formed and released.

The induced-fit hypothesis

The hypothesis suggested that the active site is flexible and is not exactly complementary to the shape of the substrate. An enzyme collides with the substrate molecule. The substrate binds to the active site.

The binding induces a slight change in the shape of the enzyme to enclose the substrate making the fit more precise. The active site now become fully complementary with the substrate as the substrate binds to the enzyme. The close fit brings the molecules in close proximity and in the correct orientation for reaction to take place. It also causes stressing and distortion of chemical bonds of the substrates. This causes the bonds to break and new bonds to form. This makes it easier for the substrate to be changed into the product, thus, lowering the activation energy required. The products formed have a different shape and are released from the enzyme. The enzyme structure is unchanged and can be reused.