Enzyme Catalysis
Mediumchemistry
Enzymes accelerate reactions by primarily:
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Solution
Incorrect! Answer:
Lowering activation energy via transition state stabilization
- Catalysis Principle: A catalyst speeds up a reaction without being consumed by providing an alternative reaction pathway.
- Activation Energy (Eaā): The energy barrier that reactants must overcome to reach the Transition State.
- Mechanism: Enzymes bind substrates in an 'active site' tailored to stabilize the Transition State (ES complex).
- Result: By reducing the energy required to reach this state, the activation energy is lowered, allowing more molecules to react at a given temperature.
- Caution: Enzymes do NOT change the equilibrium constant (no change in ĪGā).
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About This Question
- Subject
- chemistry
- Chapter
- biomolecules
- Topic
- enzyme catalysis
- Difficulty
- Medium
- Year
- 2025
This medium difficulty chemistry question is from the chapter biomolecules, covering the topic of enzyme catalysis. It appeared in the 2025 exam. Practice this and similar questions to strengthen your understanding of biomolecules concepts.
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