Enzymes

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Last updated 12:53 PM on 3/9/26
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60 Terms

1
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What does an enzyme do?

Catalyze biochemical reactions by lowering activation energy

2
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Which three bonds can form between polypeptides in a tertiary protein structure, creating its shape?

Hydrogen bonds, ionic bonds, disulfide bridge

3
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What is metabolism?

The sum of all chemical reactions occurring in a cell or organism

4
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Why are enzymes essential for metabolism?

They allow metabolic reactions to occur fast enough at normal body temperatures

5
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How do enzymes affect structure and function?

Their specific tertiary structure determines their function

6
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Why would metabolism be impossible without enzymes?

Most reactions would be too slow due to high activation energy

7
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What is an intracellular enzyme?

An enzyme that catalyses reactions inside cells

8
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Give an example of an intracellular enzyme

Catalase

9
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What reaction does catalase catalyse?

The breakdown of hydrogen peroxide into water and oxygen

10
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What is an extracellular enzyme?

An enzyme that catalyses reactions outside cells

11
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Give an example of an extracellular enzyme

Amylase

12
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What reaction does amylase catalyse?

The breakdown of starch into maltose

13
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Why are digestive enzymes extracellular?

Digestion occurs outside cells in the gut lumen

14
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What is an active site?

The region of an enzyme where the substrate binds

15
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induced fit model of enzyme action,

16
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Why are enzymes specific?

The active site is complementary to the substrate

17
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What is an enzyme–substrate complex?

A temporary complex formed when a substrate binds to an enzyme

18
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What is an enzyme–product complex?

A complex formed just before products are released

19
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What happens to the enzyme after product release?

It is unchanged and can be reused

20
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What does the lock-and-key hypothesis state?

The substrate fits exactly into the active site

21
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What is a limitation of the lock-and-key model?

It does not explain flexibility of the active site

22
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What does the induced-fit hypothesis state?

The active site changes shape when the substrate binds

23
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Why is induced-fit considered more accurate?

It explains enzyme flexibility and specificity

24
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What is activation energy?

The minimum energy needed for a reaction to occur

25
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How do enzymes lower activation energy?

By stabilising the transition state and forming enzyme

26
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Do enzymes change the overall energy of a reaction?

No, they only lower activation energy

27
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How does temperature affect enzyme activity at low temperatures?

Molecules have less kinetic energy and fewer collisions occur

28
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Why does enzyme activity increase with temperature initially?

Increased kinetic energy leads to more enzyme–substrate collisions

29
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Why does enzyme activity decrease above the optimum temperature?

The enzyme denatures

30
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What does denaturation mean?

The tertiary structure changes and the active site loses shape

31
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What is the temperature coefficient (Q10)?

The factor by which reaction rate increases for a 10°C rise

32
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What is the Q10 formula?

Q10

33
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What is the typical Q10 value for enzyme-controlled reactions?

About 2

34
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Why does pH affect enzyme activity?

It alters ionic and hydrogen bonds in the enzyme

35
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What happens if pH is too high or too low?

The enzyme may denature

36
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Why do different enzymes have different optimum pH values?

They function in different environments

37
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Why does enzyme activity increase as substrate concentration increases?

More frequent enzyme–substrate collisions

38
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Why does enzyme activity eventually plateau?

All active sites are occupied

39
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What is the maximum rate of reaction called?

Vmax

40
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What happens if enzyme concentration is increased (substrate in excess)?

Rate of reaction increases

41
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Why does increasing enzyme concentration increase rate?

More active sites are available

42
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Why are serial dilutions used in enzyme experiments?

To create a range of concentrations accurately

43
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Why must variables be controlled in enzyme experiments?

To ensure valid and reliable results

44
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Why is a water bath used in temperature investigations?

To maintain a constant temperature

45
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What is a cofactor?

A non-protein substance required for enzyme activity

46
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Give an example of an inorganic cofactor

Chloride ions

47
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Which enzyme requires chloride ions as a cofactor?

Amylase

48
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What is a coenzyme?

An organic molecule that assists enzyme action

49
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What are vitamins often used for in enzymes?

As sources of coenzymes

50
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What is an enzyme inhibitor?

A substance that reduces enzyme activity

51
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What is a competitive inhibitor?

A molecule that binds to the active site

52
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Why does a competitive inhibitor reduce enzyme activity?

It competes with the substrate

53
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How can competitive inhibition be reduced?

By increasing substrate concentration

54
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What is a non-competitive inhibitor?

A molecule that binds away from the active site

55
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Why does a non-competitive inhibitor reduce enzyme activity?

It changes the shape of the active site

56
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Can non-competitive inhibition be reversed by adding substrate?

No

57
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What is reversible inhibition?

Inhibitor can detach from the enzyme

58
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What is irreversible inhibition?

Inhibitor permanently binds to the enzyme

59
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What is end-product inhibition?

When the final product inhibits an earlier enzyme in a pathway

60
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Why is end-product inhibition important?

Prevents overproduction and saves energy

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