biological reactions are regulated by enzymes

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21 Terms

1
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How does temperature affect enzyme activity?

Activity increases with temperature as particles gain kinetic energy, but above the optimum, enzymes denature as bonds break

2
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What does “denaturation” mean?

A permanent change in an enzyme’s tertiary structure, causing the active site to lose its specific shape.

3
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How does pH affect enzyme activity?

Changes in pH alter charges on amino acids, disrupting hydrogen and ionic bonds — the active site shape is altered and substrate binding is reduced.

4
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What happens when the enzyme or substrate concentration increases?

The rate of reaction increases until a limiting factor is reached — eventually, the rate plateaus when all active sites are occupied.

5
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What is an enzyme inhibitor?

A substance that decreases or stops enzyme activity by interfering with substrate binding or catalysis.

6
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What is competitive inhibition?

A molecule similar in shape to the substrate competes for the active site — inhibition can be overcome by increasing substrate concentration.

7
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What is non-competitive inhibition?

The inhibitor binds to an allosteric site (not the active site), changing the enzyme’s shape so the substrate can no longer bind — cannot be overcome by more substrate.

8
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What is end-product inhibition?

When the final product of a metabolic pathway inhibits an enzyme earlier in the pathway, preventing overproduction.

9
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What is a cofactor?

A non-protein substance that helps an enzyme function properly — can be inorganic ions or organic molecules

10
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What are coenzymes?

Organic cofactors that temporarily bind to the enzyme and transfer chemical groups between reactions (e.g. NAD⁺, FAD).

11
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What is a prosthetic group?

A tightly bound cofactor that forms a permanent part of the enzyme (e.g. Zn²⁺ in carbonic anhydrase)

12
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Give an example of how cofactors assist enzymes

Cl⁻ ions act as cofactors for amylase, allowing the enzyme to maintain its correct shape.

13
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What is a metabolic pathway?

A series of enzyme-controlled reactions where the product of one reaction becomes the substrate for the next

14
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Why are metabolic pathways regulated?

To control the rate of product formation and maintain balance in the cell’s chemistry (homeostasis).

15
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How are enzymes used in industrial processes?

They catalyse reactions under mild conditions, saving energy and increasing efficiency in industries like brewing and biotechnology

16
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What are immobilised enzymes?

Enzymes fixed to a solid support or trapped in a gel, allowing reuse and easier separation from the reaction mixture.

17
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What are advantages of immobilised enzymes?

Increased stability, reusability, and easy product purification.

18
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Give an example of an immobilised enzyme used commercially.

Lactase, used to break down lactose in milk for lactose-intolerant individuals.

19
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What variables must be controlled in enzyme experiments?

Temperature, pH, substrate concentration, and enzyme concentration.

20
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How is enzyme activity commonly measured?

By recording the rate of product formation or substrate disappearance over time.

21
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What is the initial rate of reaction?

The fastest rate observed at the start of a reaction when substrate concentration is highest