Enzymes Flashcards

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0
Q

What do enzymes do?

A

All enzymes, though through varying reaction mechanisms work in the same basic way, by lowering the activation energy for a reaction. Allowing reactions to occur at temperatures below 40°C allowing complex, delicate organic molecules to exist.

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1
Q

What is an enzyme?

A

A globular tertiary protein that speeds up a chemical reaction without itself undergoing any change. (Are biological catalysts)

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2
Q

What is activation energy?

A

The energy needed for a reaction to occur.

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3
Q

What is “the active site” and it’s function in an enzyme?

A

This is part of the overall 3D shape of the enzyme into which a substrate can fit. This site is how an enzyme works and can be easily deformed by pH and temperature changes.

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4
Q

What does the induced fit hypothesis suggest?

A

This suggests that the active site is a flexible structure which moulds itself around a range of similar substrate shapes as they enter the active site meaning that each enzyme can react with a wider range of substrate molecules.

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5
Q

What is the first stage in the way enzymes work?

A

An enzyme and substrate collide.

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6
Q

What is the second stage in the way enzymes work?

A

The shape of the enzyme ensures the substrate moves across the enzymes surface until it enters the active site.

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7
Q

What is the third stage in the way enzymes work?

A

As it enters the active site the flexible shape of the active site moles itself around the substrate forming an enzyme-substrate complex.

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8
Q

What is the fourth stage in the way enzymes work?

A

When the enzyme-substrate complex is formed the activation energy is lowered and the reaction occurs.

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9
Q

What is the fifth stage in the way enzymes work?

A

After the reaction the substrate changes in some way. As a result of which it no longer fits the active site and falls out as a product.

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10
Q

What does Kinetic Theory state and how is this relevant to enzymes.

A

That for a chemical reaction to occur molecules have to collide. Enzyme and substrate molecules will collide when they are in solution.

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11
Q

By extension of the Kinetic Theory what does a Enzyme-Substrate reaction require?

A

Movement requires energy which is provided in the form of latent heat from the environment.

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12
Q

How does heat affect a enzyme-substrate reaction.

A

The more heat there is, the more collisions and therefore the more product is formed so the reaction goes faster.

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13
Q

How can the rate of collisions between enzymes and substrate be sped up?

A

1 - Temperature increase
2 - Increase in enzyme concentration
3 - Increase in substrate concentration

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14
Q

Describe the general trend seen between temperature and rate of reaction.

A

They are directly proportional as on average (between 0°C and 40°C) every 10°C rise causes the reaction rate to double.

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15
Q

What happens to the graph of Rate of reaction against temperature as it approaches 40°C

A

The gradient of the graph begins to decrease as the active sites are beginning to get full.

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16
Q

What happens to the graph of Rate of reaction against temperature when it hits 40°C

A

The rate of reaction is at its maximum (gradient is 0) as all active sites are fully occupied. So the enzyme concentration has become the limiting factor.

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17
Q

What happens to the graph of Rate of reaction against temperature above 40°C

A

The rate of reaction falls sharply as hydrogen and then ionic bonds start to break, denaturing the enzyme.

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18
Q

Describe the general shape of a graph of Enzyme concentration against rate of reaction.

A

It increases in direct proportion and eventually levels off when substrate concentration becomes a limiting factor.

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19
Q

Explain the initial direct proportionality seen in a graph of enzyme concentration against rate of reaction.

A

Because the collision rate increases between the enzyme and substrate.

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20
Q

How can the rate be further increased after levelling off in a enzyme concentration against rate of reaction graph

A

It can be further increased by increasing the substrate concentration.

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21
Q

Describe the general shape of a substrate concentration vs rate of reaction graph.

A

It increases in direct proportion and eventually levels off when enzyme concentration becomes a limiting factor.

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22
Q

Explain the initial direct proportionality seen in a graph of substrate concentration against rate of reaction.

A

Because the collision rate increases between the enzyme and substrate.

23
Q

How can the rate be further increased after levelling off in a substrate concentration against rate of reaction graph

A

It can be further increased by increasing the enzyme concentration.

24
Q

Describe the trend seen when measuring pH against rate of reaction and draw a conclusion from this.

A

The graph peaks about an optimum pH and drops sharply on either side, it is symmetrical about the optimum.

Meaning they are more sensitive to pH changes than to temperature

25
Q

Give an example of an enzyme that has an optimum pH of 2.0?

A

Pepsin.

26
Q

Give an example of an enzyme that has an optimum pH of 9.0?

A

Lipase

27
Q

What group of enzymes has a pH optimum of 7.0?

A

Intracellular enzymes.

28
Q

How does pH control enzymes?

A

By removing or adding electrons to the protein causing a shape change which results in temporary (until pH returns to normal) enzyme deactivation.

29
Q

What are most enzyme reactions classified as?

A

Reversible reactions.

30
Q

What does the direction of the reversible reaction depend on?

A

The balance of substrate to product.

31
Q

In the reaction A⇆B what happens if [A]>[B]

A

More B is produced.

32
Q

In the reaction A⇆B what happens if [A]=[B]

A

The reaction has reached dynamic equilibrium.

33
Q

In a cell, what do enzyme reactions tend to occur in and give an example.

A

They tend to occur in series.

E.g A⇆B⇆C⇆D⇆E

34
Q

What are these series’s also known as?

A

Metabolic pathways.

35
Q

In the metabolic pathway A⇆B⇆C⇆D⇆E what are A, E and B⇆C⇆D known as, giving examples?

A

A is the original substrate I.e retinol
B is the final product I.e pigment in the retina

B⇆C⇆D are known as intermediates.

36
Q

In the metabolic pathway A⇆B⇆C⇆D⇆E what is the condition for the reaction to continue “moving” left to right?

A

The original substrate (A) must be higher in concentration than the final product (E).

37
Q

How can a cell control metabolism in the cell?

A

By controlling enzyme production.

38
Q

What are enzyme inhibitors?

A

They are molecules which either slow down or stop specific enzymes from working.

39
Q

What is competitive inhibition caused by?

A

By molecules that have a similar shape to an enzymes normal substrate.

40
Q

Give an example of competitive inhibition.

A

Enzyme: succinic dehydrogenase
Substrate: succinate
Product: fumarate
Inhibitor: malonate.

41
Q

In competitive inhibition what is the degree of inhibition controlled by?

A

The balance of substrate to inhibitor concentration.

I.e rate = [S][I] where s=substrate and I=inhibitor.

42
Q

What is the alosteric site?

A

A secondary active site which exists by chance and which fits an non-competitive inhibitor.

43
Q

What happens when an non-competitive inhibitor bonds to the alosteric site?

A

This causes a permanent shape change to the enzyme including the shape of its active site. As a result the substrate either becomes locked into the active site or falls out unchanged and the enzyme stops working.

44
Q

In non-competitive inhibitor what does the degree of inhibition depend on?

A

Inhibitor concentration only.

45
Q

Give some examples on non-competitive inhibitors.

A

Heavy metals, cyanide, herbicides, pesticides and chemicals used in chemical warfare.

46
Q

What are immobilised enzymes?

A

These are enzymes attached to an inert, insoluble matrix.

47
Q

What material is commonly used as a matrix and how is it formed?

A

Calcium Alginate is commonly used. This is a solid, fibrous and gelatinous material. It is formed when calcium salts are added to sodium Alginate.

48
Q

How are Alginate beads formed?

A

Liquid sodium Alginate is mixed with calcium salts and the liquid is pushed through a syringe to form beads which quickly solidify.

49
Q

What are the advantages of immobilising enzymes in terms of reaction kinetics

A

As only one particle is moving when enzyme-substrate collisions occur, the kinetic energy is lower, reducing collision energy and preventing damage to the enzyme. So immobilised enzymes are more stable in terms of temperature changes allowing them to continue working up to about 70°C, allowing more product to be formed in a shorter time.

50
Q

What advantages do immobilised enzymes provide in terms of the economy of a industrial process?

A

Because an immobilised enzyme cannot move it will not be present in the produce so there is a zero purification cost.

The process of purification usually destroys the enzyme so it cannot be reused, however immobilised enzymes can be reused as there is no purification required so only a tiny a punt of enzyme is needed.

51
Q

What is entrapment (immobilised enzymes)?

A

This is a means of immobilising an enzyme by trapping it in a meshwork of fibres so it becomes physically trapped. This is the method of immobilisation found in Alginate beads. However this means that it is possible for the enzyme to escape and time is needed for the for the substrate to penetrate the beads. Finally, the active site of the enzyme may be blocked.

52
Q

Give two uses of immobilised enzymes.

A

To produce lactose free milk for adults. This is done by using Alginate beads with immobilised lactase which converts lactose into glucose and galactose.

To make concentrated fruit juice using immobilised pectinase which breaks down the calcium pectate between plant cells. The result is a fluid containing separated cells which can be crushed and all the juice retrieved.

53
Q

How can the problems associated with entrapment be solved?

A

By chemically bonding the enzyme to the surface of the bead by means of covalent cross-linkages.

54
Q

What are the uses of immobilised enzymes In Medicine?

A

Biosensors.

55
Q

Give a type of biosensor.

A

The glucose biosensor to detect diabetes.

56
Q

How does a glucose biosensor work?

A

Immobilised glucose oxidase catalysts the reaction between oxygen and glucose to form gluconic acid and hydrogen peroxide.

  1. ) the gluconic acid is directly proportional to the amount of glucose in solution.
  2. ) The greater the concentration the lower the pH and the more hydrogen ions there are.
  3. ) the enzyme is immobilised on one side of a plastic membrane so that an electrical potential difference develops because the amount of gluconic acid is greater on the side with the enzyme.
  4. ) by placing the two poles of a micro electrode either Side of the membrane the voltage can be detected and changed to a current by a transducer and a digital readout is produced.

Hence this can be applied to any acid producing reaction.