Topic 5: Enzymes And Metabolism Flashcards

1
Q

What is metabolism?

A

The sum of chemical reactions that take place in an organism, including catabolism and anabolism.

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2
Q

What is catabolism?

A

The breaking down reactions in an organism, (e.g. respiration). Energy is required.

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3
Q

What is anabolism?

A

The building up reactions in an organism (e.g. hydrolysis, photosynthesis). Energy is released.

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4
Q

What is activation energy?

A

The energy supplied to the reactants before a reaction can occur

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5
Q

What is the role of enzymes in metabolism?

A

Enzymes are present in our body and function as biological catalysts. They lower the activation energy so that chemical reactions take place at body temperature at a faster rate.

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6
Q

What is the lock and key hypothesis?

A

A hypothesis to explain the specificity of enzyme actions: An enzyme molecule only binds to substrate molecules that fit the shape of its active site.

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7
Q

Describe the process of a metabolic reaction.

A
  1. A metabolic reaction begins when the substrate molecules bind to the active site of an enzyme to form an enzyme-substrate complex.
  2. Its formation lowers the activation energy of the reaction.
  3. The substrates are converted into products.
  4. The enzyme molecule is released in its original form.
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8
Q

What components of an enzyme do the lock and key hypothesis refer to?

A

The lock refers to the substrate as they are broken down/built up during the process.
The key refers to the enzyme as it does not change during metabolism.

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9
Q

What are the properties of enzymes?

A
  1. Enzymes are biological catalysts
  2. The actions of enzymes are specific
  3. Enzymes are protein in nature
  4. Enzymes are reusable
  5. Enzymes are needed in relatively small amounts
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10
Q

Enzymes are biological catalysts.

A

Enzymes speed up metabolic reactions by lowering the activation energy of the reactions.

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11
Q

The actions of enzymes are specific.

A

An enzyme only acts on substrates that fit into its unique active site.

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12
Q

Enzymes are protein in nature.

A

The structure and activity of enzymes are easily affected by temperature and pH. They can be denatured.

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13
Q

Enzymes are reusable.

A

Enzymes remain unchanged after reactions. They can bind to other substrate molecules after the reaction is complete.

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14
Q

Enzymes are needed in relatively small amounts.

A

Since enzymes can be reused, they are usually needed in small amounts only.

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15
Q

Factors affecting rate of enzymatic reactions (3)

A
  1. Temperature
  2. pH
  3. Inhibitors
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16
Q

What happens when enzymes are exposed to low temperatures?

A

Enzymes are inactive. The chances for enzyme and substrate molecules to collide together is low.
Less enzyme-substrate complex is formed per unit time.
Therefore, the reaction rate is low.

17
Q

What happens when enzymes are exposed to higher temperatures?

A

Enzymes are more active.
Both enzyme and substrate molecules move around more rapidly and collide with each other more frequently.
This increases the chances of forming enzyme-substrate complexes.
The reaction rate increases.

18
Q

When will the rate of enzymatic reaction reach its maximum?

A

At its optimum temperature.

19
Q

What happens when enzymes are exposed to overly high temperatures?

A

High temperatures may cause confrontational change (a change in shape) of the active site of the enzyme.
The enzyme is denatured.
The substrate molecule cannot fit into the active site of the enzyme (loses catalytic ability permanently).
The rate of enzymatic reaction decreases.

20
Q

What happens when enzymes are exposed to unsuitable pH?

A

Most enzymes work in a narrow range of pH, best at their optimum pH.
The unsuitable pH will cause the enzyme to be denatured.
The rate of enzymatic reaction decreases.

21
Q

What is an inhibitor?

A

Inhibitors are chemicals that decrease the rate of enzymatic reactions.

22
Q

Examples of inhibitors?

A
  1. Cyanide
  2. Heavy metals (mercury ions, lead (II) ions, copper (II) ions)
23
Q

What are the different types of inhibitors?

A
  1. Inhibitors that are structurally similar to the substrate
  2. Inhibitors that are structurally not similar to the substrate
24
Q

How do inhibitors similar to the substrate work?

A

The inhibitor binds to the active site of the enzyme.
It competes with the substrate for the active site.
The substrate cannot bind to the active site to form enzyme-substrate complexes.

*If the concentration of enzymes increases, the competition relaxes and some enzyme-substrate complexes can be formed.

25
Q

How do inhibitors not similar to the substrate work?

A

The inhibitor binds to the other side of the enzyme. (NOT active site)
The 3D conformation of the enzyme is changed.
It is no longer complementary to the substrate.
The substrate cannot fit into the active site.
There is no enzyme-substrate complex formation.

26
Q

How are enzymes used in the food industry?

A
  1. Cheese making: Protease from young cows are used to coagulate milk to produce cheese.
  2. Fruit juice extraction:
    Pectinase can break down pectin in plant cell walls to increase the yield of juice extraction.
    It can break down pectin in the juice so it looks clear.
  3. Liquid-centred chocolate production: Invertase helps break down sugars into soluble forms, so solid sugar fillings turn into liquid upon storage.
27
Q

How are enzymes used for environmental protection?

A

Biodegradable plastic production: An enzyme extracted from a bacterium shortens the time for a plastic bag to degrade by breaking plastic down.

28
Q

Papain: cosmetics and cooking

A

Papain breaks down dead cells in skin. It makes skin softer and smoother.

Papain, a protease from papayas, breaks down protein in meat so it becomes softer.

29
Q

Cellulase: biofuel production and stonewashed jeans production

A

Cellulase breaks down cellulose fibres in jeans to produce a stone washing effect.

Cellulase is used to increase the yield in bioethanol production to break down cellulose in crops to sugars.

30
Q

Proteases and lipases: biological washing powders

A

Breaks down insoluble proteins and lipids in stains into soluble products to be removed by water.

31
Q

Lysozyme: as drugs

A

used as a drug to treat bacterial infections by breaking down the cell wall of bacteria.

32
Q

Benefits of using enzymes in the commercial industry?

A
  1. Enzymes speed up chemical reactions: shortens time for mass production
  2. Enzymes work under moderate conditions: lowers cost of production
  3. Enzymes are specific in action: fewer unwanted products
  4. Enzymes are reusable and only needed in small amounts: lowers the cost of production
33
Q

Identify the graph for the enzymatic reactions against temperature.

A
34
Q

Identify the graph for enzymatic reactions against pH.

A
35
Q

Identify the graph for enzymatic reactions against inhibitors.

A
36
Q

What is the significance of enzymatic reactions?

A

Removing toxic by products in our body.
E.g. toxic hydrogen peroxide is catalysed by catalase into oxygen and water 10^14 times faster.
This prevents it from accumulating and killing our cells.

37
Q

Draw a set up to collect and measure the volume of oxygen released during the reaction.

A