Mode of action of enzymes
Mode of action of enzymes
Basic Facts about Enzymes
- Enzymes are biological catalysts that speed up biochemical reactions in the body.
- They’re made of proteins and are highly specific, meaning each type of enzyme can only catalyse one reaction.
- Enzymes aren’t consumed in the reaction and can be used repeatedly.
- They are sensitive to changes in temperature and pH, showing optimal activity under specific conditions.
The Lock and Key Model
- Each enzyme has an active site which fits the shape of a specific substrate.
- This follows the lock and key model: the active site (the lock) can only be ‘opened’ by the correct substrate (the key).
Induced Fit Model
- The induced fit model elaborates on the lock and key, suggesting active sites are more flexible.
- On collision with the substrate, the enzyme slightly changes its shape (conformational change) to achieve a tighter fit.
- This shape change induces stress on the substrate’s bonds, facilitating the reaction.
Mode of Action of Enzymes
- Enzymes bind to their substrate forming an enzyme-substrate complex.
- This binding often involves H-bonds or ionic interaction between the substrate and R groups in the enzyme’s active site.
- After the reaction completes, the enzyme releases the products, then returns to its original conformation.
- Enzymes can speed up reactions by:
- Lowering the activation energy needed for a reaction to occur.
- Bringing two substrates together in the right orientation to react.
- Inducing a conformational shift in the substrate to destabilise existing bonds.
Effects of Environmental Factors
- Temperature: Enzyme activity increases with temperature until a peak (optimal temperature), after which the enzyme denatures and loses its function.
- pH: Each enzyme has an optimal pH at which it performs best. Variation from this pH could cause denaturation.
- Enzyme concentration: Enzyme activity increases with concentration, provided there’s enough substrate.
- Substrate concentration: If enzyme concentration is constant, activity increases with substrate concentration until a saturation point where all the enzymes’ active sites are occupied.