2.5 Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What are enzymes?

A

Enzymes are biological catalysts. They are globular proteins that can speed up a biochemical reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the active site of an enzyme?

A

-A region of an enzyme molecule where the substrate molecule binds.

-Only one type of substrate fits into the active site. This is what is meant by enzyme-substrate specificity: one enzyme can only catalyze one type of reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the active site a result of?

A

-The folding of the polypeptide chain(s).

-The resulting (3D) shape that is formed by the polypeptide chain forms the active site, which is where the substrate interacts with the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Diagram showing a substrate entering the active site of an enzyme.

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What happens when the substrate binds to the enzyme’s active site?

A

-The enzyme changes shape slightly.

-This ‘induced fit’ results in tighter binding of the substrate to the active site.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Structure of enzymes

A

Large globular polypeptides with a tertiary or quaternary structure.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

When describing an enzyme structure, don’t forget to mention an ___

A

Active site and specificity of enzymes as well as the fact that all enzymes are globular proteins.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

The reaction that converts the substrate into the products takes place in ___

A

The active site of the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

When the substrate enters the active site, it triggers a change in ___

A

-The three-dimensional shape of the enzyme that allows a tighter fit.

-This is called an induced fit and is possible because of the flexibility of the protein molecules that make up the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

When the enzyme and substrate(s) fit together tightly, the enzyme induces ___

A

The weakening of bonds within the molecules of the substrate(s), thus reducing the activation energy needed for the reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

When the enzyme-catalysed reaction is completed, ___

A

The products are released from the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

The induced fit theory has replaced the ___

A

Lock and key theory

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

According to the lock and key hypothesis, ___

A

-The enzyme functions as a lock while the substrate functions as a key.

-There is a perfect matching between both components.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The induced fit model suggests that ___

A

-A substrate is capable of inducing a change of the active site that will enable the enzyme to perform its catalytic function.

-The active site can slightly change its shape to fit a substrate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Diagram showin the induced fit model (how a substrate enters the active site of an enzyme, the enzymatic reaction occurs and the products are released from the enzyme.)

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Key points about enzymes

A

1) An enzyme is a globular protein that acts as a catalyst for a (bio)chemical reaction.

2) An active site is the region of an enzyme to which substrates bind and where reactions are catalysed.

3) Enzymes are specific: they catalyse only one type of reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is an active site?

A

A region of an enzyme molecule where the substrate molecule binds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What does enzyme–substrate specificity mean?

A

Enzymes can only catalyse one type of reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

How do enzymes speed up a reaction?

A

By lowering the activation energy of that reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Diagram showing how enzymes lower the activation energy of a reaction

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Define activation energy

A

The minimum energy that reacting particles should possess in order for a reaction to occur.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is a catalytic reaction?

A

When an enzyme converts the substance into products, such as when amylase hydrolyses starch to produce di- and monosaccharides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What kind of motion does enzyme catalysis involve?

A

Molecular motion and the collision of substrates with the active site.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

The motion of atoms and molecules in a liquid is very ___

A

Random and depends on the tempeture.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

In humans, where the body temperature is around 37   °C, the movement of atoms and molecules is ___

A

Rapid and many millions of collisions take place every second.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

When is catalysis of a reaction only possible?

A

If the substrate and active site happen to be correctly aligned when they collide to allow binding to take place.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Exothermic or exorgonic reaction

A

A reaction where product formation is associated with release of energy, usually in the form of heat.

28
Q

Enrothermic or endergonic reaction

A

A reaction where product formation is associated with absorption of energy, usually in the form of heat.

29
Q

All enzymes are proteins. Therefore, they can be ___

A

-Denatured and lose their catalytic properties.

-The bonds between different amino acids break, causing structural changes to the active site of an enzyme.

30
Q

What factors can cause denaturation?

A

1) Temperature

2) pH

3) Substrate concentration

4) Enzyme concentration

31
Q

Effect of temperature on enzymes

A

-Enzymes are sensitive to temperature changes.

-When temperature is low, molecules tend to move slowly.

-The chance of collision between substrate and enzyme molecules is also low.

-When temperature rises, molecules move more rapidly and it is more likely that they will collide with each other.

-Each enzyme has an optimum temperature in which the rate of enzymatic reaction is the highest.

-The optimal temperature for human enzymes is around 37   °C.

-Interestingly, for enzymes in the bacterium Thermus thermophilus that lives in hot springs the optimal temperature is 65   °C.

-If the temperature is higher than optimal, an enzyme can be denatured.

-As a result, the rate of enzymatic reaction rapidly decreases.

32
Q

Graph showing effect of temperature on enzymes

A
33
Q

Where do most enzymes have their optimal temperature?

A

Around 40°C

34
Q

Effect of substrate concentration on enzyme

A

-When the substrate concentration is low, there are more enzyme molecules available than substrate.

-The rate of reaction is relatively low.

-Increasing the substrate concentration causes more chances of collision between substrate and enzyme molecules.

-Hence, the rate of enzymatic reaction rises gradually.

-However, this increase is halted when all active sites are occupied by substrate molecules.

-After this point, adding more substrate does not affect the rate of reaction. (V max is the maximum rate possible).

-Once V max is reached (the maximal rate of reaction), substrates have to wait for enzyme active sites to become available before they can bind.

35
Q

Graph showing the effect of substrate concentration on enzyme activity.

A
36
Q

Effect of pH on enzymes

A

-Enzymes work in different environments.

-Examples include the stomach, where the pH is very low (pH = 2), and the small intestine, which is more alkaline (pH = 7.5).

-Figure 3 shows two enzymes: pepsin and trypsin.

-Pepsin is an enzyme produced in the stomach, whereas trypsin is formed in the small intestine.

-Each enzyme has its own optimum pH at which its activity is the highest.

37
Q

Effect of pH on pepsin (red line) and trypsin (blue line)

A
38
Q

How can extreme pH values denature an enzyme?

A

-By altering the three-dimensional structure of its active site.

-If pH is lower or higher than the optimal, the rate of reaction gradually decreases.

39
Q

Drawing graphs to show the expected effects of temperature, pH and substrate concentration on the activity of enzymes.

A

-When sketching graphs you should remember the shape of each curve.

-For temperature, the rate of enzymatic reaction drastically drops after reaching the optimal temperature.

-When you sketch a rate of reaction for different substrate concentrations don’t forget to draw a plateau phase in which the rate remains constant.

40
Q

Denaturation is an ___ change

A

Irreversible

41
Q

Denaturation destroys the ___

A

-Tertiary or quaternary conformation of a protein.

-In some cases, when the temperature is high enough or the pH is extreme, the secondary structure of a protein can be altered.

42
Q

When there is only a minor temperature increase or change in pH, it is possible that ___

A

The denaturation is still reversible and the protein can fold back to its original and functional conformation.

43
Q

Diagram denaturation of a protein a protein (loses its conformation with denaturation. The beta sheets and alpha helices lose their form, and the protein reverts to a primary conformation. This means there is no longer a functional active site.)

A
44
Q

Examples of enzymes in every-day life.

A

1) Proteases are used to produce milk powders for babies and carbohydrase helps to manufacture corn syrup.

2) Enzymes are widely used in industries such as medicine, fuels, agriculture and even production of textiles.

3) Brewing, baking and cheese-making are the most common processes in which enzymes play a crucial role.

45
Q

What needs to happen for enzymes to be made mode stable and useful?

A

They need to be immobilised

46
Q

What is immobilisation?

A

The process of attaching an enzyme to a material so that its movements are restricted.

47
Q

Advantages of immobilisation

A

-For example, if enzymes are not immobilised, they are often present in the final product, which restricts the concentration that can be used to process food for human consumption to avoid adverse effects.

-The use of immobilised enzymes permits higher concentrations of enzymes to be used, allowing a faster rate of reaction.

-Moreover, immobilisation of enzymes allows immediate separation of the enzymes from the reaction mixture, which allows them to be recycled, reducing production costs.

48
Q

Use of enzymes in industry

A

-Protein hydrolysis

-Detergent

-Food processing

49
Q

Use of enzymes in the environment

A

-Degredation of residual waste

-Detoxification of toxic substances

50
Q

Use of enzymes in agriculture

A

-Feed processing

-Animal feed additive

-Agroprocessing

51
Q

What industries can enzymes be used in?

A

-Industry

-Environment

-Agriculture

52
Q

What is lactose?

A

-Lactose is a naturally occurring disaccharide present in mammalian milk and dairy products such as cheese and yogurt.

-It consists of two monosaccharides: glucose and galactose.

53
Q

What is lactase?

A

An enzyme that can break down lactose into monosaccharides.

54
Q

Diagram of lactase breaking down lactose into galactose and glucose

A
55
Q

What does lactase break down lactose into?

A

Galactose and glucose

56
Q

Lactose intolerance: Lack of lactase causes ___

A

Lactose to build up and remain in the digestive system, where it is fermented by bacteria.

57
Q

Lactose-intolerant people should consume lactose-free products to avoid ___

A

Gastric problems caused by the excess of undigested lactose in the alimentary gut.

58
Q

Advantages of the production of lactose-free products

A

-No ill effects after consumption

-Quicker fermentation, for example, in yogurt production as bacteria ferment glucose and galactose more readily than lactose

-Sweeter tasting milk (glucose and galactose are sweeter tasting than lactose).

59
Q

How are lactose-free products produced?

A

-By adding the enzyme lactase (usually made on industrial scale from the fungus Aspergillus niger) to milk.

-Lactase breaks down lactose into its constituent monomers, glucose and galactose.

60
Q

Explain how lactase can be immobilized

A

-Lactase can be immobilized in alginate beads, while the milk is allowed to flow past

-With this method, no lactase ends up in the final dairy product, making it better for consumption.

61
Q

Diagram showing the production of lactose-free milk by using immobilized enzymes.

A
62
Q

Yogurt is tolerated better than milk by lactose-intolerant people because ___

A

Lactase from the bacteria in yogurt helps digest the lactose.

63
Q

Immobilized enzymes are used in industry because ___

A

Enzymes can be recycled and used several times.

64
Q

2.5.6

A
65
Q

Enzyme and substrate: reaction steps - diagram

A
66
Q

Where is lactase produced?

A

By cells in the lining of the small intestine.