Classifying each of the characteristics as a lock-and-key model or induced-fit model or both based on the fact that in the "lock-and-key" theory, an enzyme's active site precisely matches a particular substrate. Whereas according to the induced fit concept, an enzyme's active site will alter conformation when it binds a substrate to enhance the fit.
According to the "lock-and-key" concept of enzyme-substrate interaction, the enzyme and the substrate have distinct complementary geometric geometries that perfectly fit one another. Enzymes are extremely specialized. Before they can catalyze a chemical process, they first need to bind to a particular substrate.
Koshland first put out the induced-fit model in 1958 to describe the protein conformational changes that take place during the binding process. According to this paradigm, an enzyme optimizes the interface through physical interactions to create the final complex structure when it binds with its substrate.
A model with Lock and Key: Active site is stiff
Induced fit Model:
- Flexible active site
- Modified substrate shape
- Active site-substrate interaction results in the best fit for catalysis
Both:
- Enzyme specificity depends on the substrate
- After catalysis, an enzyme reverts to its original state
Learn more about lock and key models and induced-fit models here:
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