Amylase is an enzyme that breaks down starch into simple sugars. Explain how the 'lock and key' hypothesis describes the way amylase acts on starch, and explain why amylase cannot break down proteins.
Written & reviewed by James Millett — Biology (Imperial College London), PGCE Science (University of Cambridge).
Model answer (5 marks)
The active site of amylase has a specific shape that fits only a particular substrate. The starch molecule has a complementary shape to this active site, so it fits exactly like a key in a lock. When the starch enters the active site, an enzyme‑substrate complex is formed and the enzyme can cleave the starch into simple sugars. Proteins, however, do not have a shape that matches the amylase active site. Consequently, no enzyme‑substrate complex can form between amylase and a protein, so the protein cannot be broken down.
Examiner tips
- Use the phrase ‘lock and key’ to show understanding of specificity
- Explain the sequence: shape match → complex formation → catalysis
- State why proteins cannot fit the active site
Common mistakes
- Confusing the lock‑and‑key model with induced fit
- Claiming amylase can act on proteins without explaining shape mismatch
- Omitting the step that no complex forms
Mark scheme (5 marks)
- The active site of amylase has a specific shape
- The starch molecule (substrate) has a complementary shape to the active site
- Starch enters the active site to form an enzyme-substrate complex
- Proteins do not have a complementary shape to the active site of amylase
- Therefore no enzyme-substrate complex can form between amylase and protein, so the protein cannot be broken down
Related
- All Eduqas A-Level Biology revision notes →
- How to answer a "Explain" question →
- Decode the mark scheme abbreviations →
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