Explain how the specificity of enzymes arises from their molecular structure, and state one consequence of this specificity for metabolic pathways.
Written & reviewed by James Millett — Biology (Imperial College London), PGCE Science (University of Cambridge).
Model answer (4 marks)
Enzymes are globular proteins whose tertiary structure gives them a specific three‑dimensional shape.
The active site is a pocket or cleft whose shape and chemical properties match those of a particular substrate, so that only that substrate can fit.
The binding is stabilised by interactions such as hydrogen bonds and ionic bonds between the R‑groups of the amino acids that line the active site and the substrate.
Because each enzyme recognises only one substrate (or a very small group of substrates), each step in a metabolic pathway is carried out by a different, specific enzyme, which allows the pathway to be tightly regulated and controlled.
The active site is a pocket or cleft whose shape and chemical properties match those of a particular substrate, so that only that substrate can fit.
The binding is stabilised by interactions such as hydrogen bonds and ionic bonds between the R‑groups of the amino acids that line the active site and the substrate.
Because each enzyme recognises only one substrate (or a very small group of substrates), each step in a metabolic pathway is carried out by a different, specific enzyme, which allows the pathway to be tightly regulated and controlled.
Examiner tips
- Show the link between tertiary structure and active‑site shape; mention complementary fit. Include at least one type of interaction (H‑bond, ionic, etc.). State the consequence clearly – specific enzymes enable precise regulation of the pathway.
- common_mistakes
- :
- Using generic terms like ‘protein’ without emphasising tertiary structure. Omitting the complementary fit or the specific interactions that stabilise the complex. Failing to state the consequence in terms of regulation or control.
Mark scheme (4 marks)
- Enzymes are globular proteins with a specific three-dimensional (tertiary) structure.
- The active site has a shape complementary to that of the specific substrate, allowing the enzyme–substrate complex to form.
- Interactions (e.g. hydrogen bonds, ionic bonds) form between R-groups / amino acids of the active site and the substrate, stabilising the complex.
- One consequence: each reaction in a metabolic pathway is catalysed by a different, specific enzyme, allowing precise regulation / control of the pathway.
Key terms in this question
metabolic pathway · specificity
Related
- All IB DP Biology Standard Level (2023 syllabus) revision notes →
- How to answer a "Explain" question →
- Decode the mark scheme abbreviations →
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