Specificity: Each enzyme (E) has a specific substrate (S) binding site within its structure.
Enzyme-Substrate Complex (ES): The binding site facilitates the formation of a highly reactive, transient (short-lived) ES complex.
Enzyme-Product Complex (EP): The ES complex transitions into an EP complex.
Product Formation and Enzyme Regeneration: The EP complex dissociates, yielding the product(s) ℗ and regenerating the unchanged enzyme (E).
Overall Reaction: E + S ⇌ ES → EP → E + P
Importance of ES Formation: Crucial for the catalytic activity of the enzyme.
Catalytic Cycle of Enzyme Action (Step-by-Step)
1. Substrate Binding:
The substrate molecule encounters the enzyme.
The substrate fits specifically into the enzyme’s active site.
Two models explain this interaction:
Lock and Key Model: The substrate perfectly fits the pre-existing active site of the enzyme, like a key in a lock.
Induced Fit Model: Substrate binding triggers a conformational change in the enzyme’s shape, allowing the enzyme to snugly fit around the substrate, maximizing interaction and stabilizing the transition state. This is the currently favored model.
2. Catalysis (Bond Breaking and Product Formation):
The active site, now in close proximity to the substrate, facilitates the breaking of chemical bonds within the substrate.
This bond breaking leads to the formation of the enzyme-product complex (EP).
The chemical transformation of the substrate occurs at this stage.
3. Product Release and Enzyme Regeneration:
The enzyme releases the newly formed product(s) ℗ from its active site.
The enzyme returns to its original conformation.
The free enzyme is now available to bind with another substrate molecule and repeat the catalytic cycle. This ensures the enzyme can catalyze multiple reactions.