enzyme catalysis

Question

Enzymes accelerate reactions by primarily:

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1. **Catalysis Principle**: A catalyst speeds up a reaction without being consumed by providing an alternative reaction pathway.
2. **Activation Energy ($E_a$)**: The energy barrier that reactants must overcome to reach the Transition State.
3. **Mechanism**: Enzymes bind substrates in an 'active site' tailored to stabilize the **Transition State** (ES complex).
4. **Result**: By reducing the energy required to reach this state, the **activation energy is lowered**, allowing more molecules to react at a given temperature.
5. **Caution**: Enzymes do NOT change the equilibrium constant (no change in $\Delta G^\circ$).

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Enzyme catalysis is an example of: