M1:08 Enzyme intro Flashcards

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

Describe the structure of a globular protein

A

it has a specific three dimensional shape or tertiary structure, with hydrophobic amino acids on the inside and hydrophilic amino acid R-groups around the outside of the ball.

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

Give 5 ways in which all enzymes are similar

A
  • they are all globular proteins, generally soluble in water- they act as catalysts, speeding up chemical reactions, but was not used up as part of the reaction- they are specific, catalysing a reaction involving only one type of substrate - the globular structure contains a pocket or cleft area are called an active site- their activity is affected by temp and pH
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How large is the active site of an enzyme in comparison to the total size?

A

very small, there are thousands of amino acids in an enzyme. (often fewer than 10 of these enzymes make up the active site)

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

What is the role of the majority of the amino acids within an amino acid?

A

they are involved in maintaining the specific tertiary structure, which enables the enzyme to function properly.

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

Name one of the main advantages to enzymes

A

they are specific to one catalytic and does not produces a range of unwanted by-products.

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

What are the main commercial applications of enzymes?

A

28% detergents 35% food processing 23% beverages

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

Give some examples of the formation and breakages of bonds that uses enzymes?

A

glycosidic bondsester bonds peptide bonds

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

Name 4 processes that use a range of different enzymes

A

respiration photosynthesisdigestion and protein synthesis

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

What does a substrate become when it is catalysed by an enzyme? and give an example

A

a producteg if you use the enzyme maltase to catalyse the conversion of maltose into glucose, then the substrate maltose is converted into glucose (the product)

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

What is the usually format for naming a specific substrate?

A

its usually derived from the substrate of the reaction that is catalysed with the suffix -ase

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

Describe the reaction catalysed by the enyzyme lactase

A

The break down of milk sugar, lactose into glucose and galactose monomers.

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

What makes lactose-intolerants, intolerant to lactose and what are the effects.

A

They do not produce lactase and it causes them to suffer stomach cramps, bloating and diarrhoea

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

Describe the reaction catalysed by the enyzyme catalase

A

The breakdown of hydrogen peroxide to water and oxygen gas. Almost all organisms produce catalase brcause hydrogen peroxide is a toxic by-product of some metabolic reactions

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

Describe the reaction catalysed by the enyzyme Ribulose biphosphate carboxylase (rubisco).

A

Plants need carbon dioxide for photosynthesis. The enzyme rubisco catalyses the binding of carbon dioxide to a molecule called ribulose bisphosphate.

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

Describe the reaction catalysed by the enyzyme ATP-ase.

A

The break down of ATP to produce ADP and a phosphate group. This reaction releases a small amount of energy that is used to drive energy requiring processes such as active transport

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

Describe the reaction catalysed by the enyzyme glycogen synthetase

A

The building up of glycogen of catalysing the joining together of glucose molecules. Glycogen is the storage carbohydrate of animals.

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

What are the weaknesses of enzymes?

A

The same as protein weaknesses, their shape must remain in tact

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

What can endothermic animals do?

A

maintain their internal body temperature independently of the environment, allowing them to live in so many enviroments all around the world

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

How does it help by regulating body temperatures in endothermic animals?

A

As it means that enzymes can function at a near optimum temperature

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

What is the advantage and disadvantage to regulating body temperatures in endothermic animals?

A

It has allowed mammals to live successfully on land and water.It requires alot of energy so mammals and birds require a lot more food than a similarly size reptile.

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

What is a heterotroph?

A

an organism that obtains its nutrients by consuming other organisms, that need to break down the body of organisms they are consuming in order to extract the nutrient molecules they need for their own growth and energy requirements.

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

Name 3 bonds that must be broken down during digestion.

A

esterpeptide glyosidic

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

`Describe the two methods of digestion

A

-Some organisms secrete enzymes out of them and then the enzymes digest molecules into their monomers, which the organism then takes in and uses - Others have internal digestive systems, that mixes enzymes with the food as it is digested (many of these enzymes are extracellular)

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

What does extracellular mean?

A

enzymes catalyse reactions outside the cell

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

What does intracellular mean?

A

Enzymes catalyse reactions inside the molecule

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

What does mould produce to digest bread?

A

extracellular enzymes

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

are enzymes just used simply as a catalyst?

A

no, they are often used as defensive mechanisms.

28
Q

Give an example of a white blood cell that use enzymes for digestion

A

phagocytes, they take in and digest bacteria using lysosomal enzymes

29
Q

How do white blood cells engulf bacterial cells?

A

An endocytosed vesicle is fused with one of the many lysosomes present and lysosomal enzymes digest the bacterium. (phagocytosis)

30
Q

What is activation energy?

A

The amount of energy that must be applied for a reaction to proceed.

31
Q

How do enzymes affect the activation energy needed?

A

They reduce it

32
Q

Is the amount of activation energy required, the same for each enzyme?

A

no, it varies

33
Q

Use maltose as an example of how enzymes break down molecules

A

The glycosidic bond must be broken and a water molecule must be split at the same time, this happens when maltose is boiled with an acid which provides the right conditions for maltose molecules to collide with water molecules ‘energetically’ enough to achieve hydrolysis (the activation energy)

34
Q

How do enzymes help a cell function?

A

they reduce the amount of activation energy needed, so reactions can proceed quickly at temperatures much lower than boiling point. (They can do this because of the way the active site is shaped to fit the substrate molecule/s)As these reactions would need a lot more energy without the enzyme

35
Q

What role does the substrate play?

A

substrates are where the reaction occurs, eg maltose may enter an enzyme, and two glucose molecules would leave as the products

36
Q

Name 2 ways its thought that enzymes work

A

lock and key induced fit theory

37
Q

Describe the lock and key theory.

A

The substrate ‘key’ fits into the active site ‘lock’. The substrate is then held in one place so the reaction can go ahead.

38
Q

Describe the induced fit theory

A

As the substrate molecule collides with the AS, the enzyme changes shape slightly which makes the active site fit more closely round the molecule and is held in place because of the opposite charges of the substrate and the active site (an enzyme-substrate complex) - This change in shape places a strain on the substrate, destabalising the molecule so the reaction occurs more easily. This produces a produce (known as the enzyme-product substrate) that is a different shape to the original substrate so no longer fits the active site.

39
Q

What is the product of an enzyme reaction called?

A

a substrate-product complex

40
Q

How does kinetic energy affect an enzyme

A

As it increases the amount of random collisions, and they collide with greater speed, and therefore greater force

41
Q

What happens to bonds when heat is applied to a solution?

A

the vibrations of the molecules put a strain of the molecules, it could even denature some structures, reducing reaction rates.

42
Q

What is denaturation?

A

the changes to the tertiary structure of an enzyme so it cannot function and its function cannot be restored (but it does not change the primary structure of an enzyme/protein ie peptide bonds arent broken)

43
Q

What happens to the rate of reaction if heat is added?

A

it will increase until the optimum rate of reaction, and after this point it reduces due to an increase in the amount of enzymes being denatured

44
Q

How do you measure the effect of temperature on enzyme action?

A

carry out enzyme controlled reactions at different temperatures , using a waterbath controlled by a thermostat, and you can measure the production of product or the disappearance of substrate in various ways (in detail later)

45
Q

What is the average range for optimum temperatures of enzymes?

A

40-50

46
Q

What is a polymerase chain reaction?

A

where heat resistant enzymes are used to catalyse reactions involved in making many copies of DNA segments (very similar to DNA replication) which is used in modern genetic engineering.

47
Q

What is pH?

A

the measure of the hydrogen concentration, with values ranging from 1-14 (1=acid, 14=alkaline)

48
Q

Do acids have a low or high concentration of H+?

A

high, the higher the concentration of hydrogen, the lower its found on the pH scale.

49
Q

What is an acid defined as in chemical terms?

A

a proton doner as hydrogen ions are also known as protons.

50
Q

Why do hydrogen bonds hold together tertiary structures?

A

As they are attracted to the negative groups on the amino acids.

51
Q

Why does the concentration of hydrogen bonds(pH) affect the tertiary structure of an enzyme molecule? What else can it affect?

A

As hydrogen ions can interfere with the hydrogen and ionic bonds that hold the tertiary structure together,also affects the shape of the active site, so can also affect the rate of enzyme controlled reactions

52
Q

How does increasing the concentration of hydrogen affect the charges round the active site?

A

As more hydrogen ions are attracted towards any negatively charged groups in the active site.

53
Q

What is the most common optimum pH level for enzymes? Why is it optimum?

A

pH 7, as it gives the tertiary structure of the enzyme the best overall shape to hold the substrate in place.

54
Q

Is the pH range for an enzyme quite broad or narrow?

A

narrow

55
Q

How is the effect of pH on an enzyme measured?

A

You carry out enzyme-controlled reactions at different pH values using buffering solutions, and the production of a product or the disappearance of a substrate can be measured in a variety of ways (seen later)

56
Q

Give examples of enzymes working at different pHs in the human digestive system

A

In the stomache, the protein digesting enzyme pepsin works at an optimum pH level of 2But then trypsin, the protein digesting enzyme in the small intestine works best at pH7

57
Q

What happens as you increase the concentration of substrates/

A

collisions between enzymes and substrate molecules occur more often , so more enzyme-substrate complexes occur

58
Q

Describe what happens at the maximum reaction rate

A

all the enzymes present are forming enzyme substrate complexes as fast as possible, so it cannot increase any further (meaning an increase in substrate will no longer have any effect)

59
Q

How do you increase the rate of reaction?

A

adding both more substrates and enzymes

60
Q

If you mixed enzymes and substrates once, and did not add anything to the solution once the reaction has begun, why would the rate of reaction increase, and then eventually decrease again?

A

As the substrate is slowly being used up, so its concentration is decreasing, while the concentration of enzymes remains the same and the concentration of products increases.

61
Q

What is the initial rate of reaction?

A

The highest reaction rate, which gives the maximum possible reaction rate for an enzyme under a particular experimental situation

62
Q

When is a factor described as a limiting factor/

A

if there is a situation where, if all other conditions kept constant, increasing the concentration of that factor alone will increase the reaction rate

63
Q

What is the plateau of a graph and why does it occur in graphs of increasing the enzyme/substrate concentration?

A

the leveling off of the graphoccurs as the level of the molecule remaining constant prevents any further increase in the reaction rate.

64
Q

What happens if the concentration of the limiting factor is increased?

A

then the reaction rate increases

65
Q

Why are enzyme concentrations often quite low in cells

A

As they are catalysts so they work over and over again, driving the same reaction.