The induced fit and lock-and-key model are two proposed models that explain how substrates may bind to the active site of an enzyme. There are several significant differences between the two models.
Induced Fit Model
Refers to an enzyme-substrate interaction model in which the active site of the enzyme does not fit the substrate completely
Shapes are not complementary before binding
The active site of the enzyme contains two components
The active site of the enzyme is not static and has to undergo a conformational change to improve binding
Binding is flexible and not very strong
A transition state develops before the reactants undergo changes
The enzyme has a separate catalytic group, which weakens the substrate bonds either by the nucleophilic or electrophilic attack
Proposed by Daniel Koshland in 1958
Lock & Key Model
Refers to an enzyme-substrate interaction model in which the active site of the enzyme precisely fits with the substrate
Shapes are complementary with each other before binding
The active site of the enzyme contains a single entity
The active site of the enzyme is static and does not undergo any conformational changes before binding
Binding is inflexible and very strong
A transition state does not develop before the reactants undergo changes
The enzyme does not have a separate catalytic group hence there is no weakening of the substrate bonds