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IMAT Bio > Chapter 4: Enzymes > Flashcards

Chapter 4: Enzymes Flashcards

1
Q

What are enzymes made of?

A

Globular proteins.

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2
Q

Why do enzymes have hydrophilic R groups on their surface?

A

To ensure they are soluble in water.

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3
Q

What is the active site of an enzyme?

A

The region where the substrate binds.

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4
Q

What does the induced fit hypothesis describe?

A

Enzymes and substrates change shape slightly to ensure a perfect fit.

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5
Q

What happens to enzymes after catalyzing a reaction?

A

They remain unchanged.

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6
Q

What is a substrate?

A

The molecule that binds to the enzyme’s active site.

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7
Q

What is an enzyme-substrate complex?

A

The temporary structure formed when a substrate binds to an enzyme.

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8
Q

How do enzymes lower activation energy?

A

By holding substrates in a position that facilitates reaction.

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9
Q

What happens to the bacterial cell wall when lysozyme acts on it?

A

It loses rigidity and the cell bursts.

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10
Q

What type of reaction does lysozyme catalyze?

A

Hydrolysis.

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11
Q

What determines an enzyme’s specificity?

A

The shape of its active site.

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12
Q

What is activation energy?

A

Energy required to start a chemical reaction.

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13
Q

What is the effect of low temperature on enzymes?

A

Slower movement of molecules and reaction rates.

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14
Q

What happens to enzymes above their optimal temperature?

A

They denature.

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15
Q

What does denaturation mean?

A

Loss of enzyme shape and function.

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16
Q

How does pH affect enzymes?

A

It alters the ionic bonds in the enzyme structure.

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17
Q

What happens to enzymes at extreme pH levels?

A

They denature.

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18
Q

How does substrate concentration affect reaction rate initially?

A

The rate increases with substrate concentration.

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19
Q

What happens when enzymes are saturated with substrate?

A

The reaction rate plateaus.

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20
Q

What is competitive inhibition?

A

An inhibitor competes with the substrate for the active site.

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21
Q

Can competitive inhibition be reversed?

A

Yes

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22
Q

What is non-competitive inhibition?

A

An inhibitor binds to an allosteric site

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23
Q

Can non-competitive inhibition be reversed by increasing substrate?

A

No

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24
Q

What is the allosteric site?

A

A site on the enzyme other than the active site.

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25
Q

What is end-product inhibition?

A

When the end product of a reaction inhibits the enzyme’s activity.

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26
Q

Why is end-product inhibition beneficial?

A

It prevents overproduction and waste of resources.

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27
Q

What are metabolic pathways?

A

Sequences of enzymatic reactions in cells.

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28
Q

What is the role of enzymes in metabolism?

A

To catalyze reactions.

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29
Q

What happens when inhibitors bind to the active site?

A

They block substrate binding.

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30
Q

How does an allosteric inhibitor affect the active site?

A

It distorts the site

31
Q

What is the maximum reaction rate?

A

The fastest rate an enzyme can catalyze a reaction.

32
Q

What limits reaction rates in enzymes?

A

Saturation of enzymes by substrates.

33
Q

What happens in a hydrolysis reaction?

A

A molecule is broken down by water.

34
Q

What prevents substrate binding in competitive inhibition?

A

The inhibitor occupies the active site.

35
Q

What type of inhibition does not depend on substrate concentration?

A

Non-competitive inhibition.

36
Q

What is negative feedback in enzyme activity?

A

Regulation where the product inhibits the process.

37
Q

What ensures enzyme solubility?

A

Hydrophilic R groups.

38
Q

What happens during enzyme denaturation?

A

The enzyme loses its functional shape.

39
Q

How do hydrogen ions affect enzymes?

A

They interact with R groups

40
Q

What is the role of enzymes in exergonic reactions?

A

To lower activation energy.

41
Q

What does the curve for non-competitive inhibition show?

A

A reduced maximum reaction rate.

42
Q

How does substrate concentration affect competitive inhibition?

A

Increased substrate outcompetes the inhibitor.

43
Q

What is the role of an allosteric enzyme?

A

To regulate metabolic pathways.

44
Q

What is the groove in lysozyme’s active site designed for?

A

Binding polysaccharide chains.

45
Q

How do enzymes speed up chemical reactions?

A

By reducing the energy barrier.

46
Q

What happens to reaction rates when enzymes are at their optimum?

A

They are at their peak.

47
Q

Why does adding substrate not always increase reaction rates?

A

Enzymes have a saturation point.

48
Q

What does ‘induced fit’ mean?

A

Enzymes adjust shape to bind substrates.

49
Q

Why are enzymes reusable?

A

They are unchanged after the reaction.

50
Q

How does a competitive inhibitor mimic the substrate?

A

By having a similar shape.

51
Q

What type of inhibition involves molecules binding away from the active site?

A

Non-competitive inhibition.

52
Q

What is a key characteristic of competitive inhibitors?

A

They compete with the substrate for the active site.

53
Q

How does end-product inhibition prevent waste?

A

By stopping overproduction of substances.

54
Q

What determines the effect of substrate concentration on competitive inhibition?

A

The ratio of substrate to inhibitor.

55
Q

How does a non-competitive inhibitor affect enzyme activity?

A

It reduces activity regardless of substrate concentration.

56
Q

What happens to the enzyme in reversible competitive inhibition?

A

The inhibitor can detach

57
Q

What is the function of the bacterial cell wall?

A

To provide rigidity and prevent bursting.

58
Q

How does lysozyme disrupt bacterial cells?

A

By breaking down polysaccharide chains in the cell wall.

59
Q

What happens in the active site during an enzymatic reaction?

A

Substrates are converted into products.

60
Q

What prevents further increase in reaction rate when enzymes are saturated?

A

All active sites are occupied.

61
Q

What does a substrate need to align with for a reaction?

A

The active site of the enzyme.

62
Q

Why can’t enzymes function in extreme pH environments?

A

Ionic bonds are disrupted

63
Q

How do enzymes achieve specificity?

A

Their active sites have unique shapes matching specific substrates.

64
Q

What happens to the rate of reaction at very low substrate concentrations?

A

It is slow due to fewer enzyme-substrate interactions.

65
Q

How does substrate binding affect the enzyme?

A

It may induce a slight change in enzyme shape.

66
Q

What is the role of enzymes in hydrolysis reactions?

A

To break down large molecules into smaller ones.

67
Q

What causes enzymes to lose their function at high temperatures?

A

Breaking of bonds maintaining their shape.

68
Q

How is the reaction rate related to enzyme concentration?

A

Higher enzyme concentration increases the rate

69
Q

What happens when an inhibitor binds to the allosteric site?

A

It causes a conformational change in the enzyme.

70
Q

How does the cell control enzyme activity in metabolic pathways?

A

Through feedback mechanisms like end-product inhibition.

71
Q

What makes non-competitive inhibition irreversible in some cases?

A

Strong binding of the inhibitor to the enzyme.

72
Q

How does the induced fit model benefit enzyme efficiency?

A

It enhances the binding between enzyme and substrate.

73
Q

What happens to the enzyme once the product is released?

A

It is free to catalyze another reaction.

IMAT Bio (11 decks)

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