Topic 2- Enzymes Flashcards

1
Q

What is Metabolism

A

The chemical reactions of an organism

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2
Q

Give 2 types of Metabolism, and distinguish between them

A

Catabolism and Anabolism
Catabolism - ‘breakdown’ reactions
Anabolism - ‘build-up’ reactions

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3
Q

What is the theory of Enzyme action

A
  1. Enzyme + substrate
  2. Enzyme - substrate complex
  3. Enzyme - product complex
  4. Enzyme + product
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4
Q

What is the definition of an Enzyme

A

A biological catalyst that speeds up the rate of reaction, without using itself up

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5
Q

How do Enzymes have specific shapes

A

It is determined by their tertiary structure

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6
Q

What is the Active site

A

The particular part of the enzyme molecule where the reaction takes place

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7
Q

How do Enzymes affect the Activation Energy

A

It lowers it, which allows the reaction to take place

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8
Q

What are Enzymes to a substrate

A

Specific

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9
Q

Give 2 models which explain how Enzymes work

A

Lock and key

Induced fit

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10
Q

Give similarities between the Induced fit model and the lock and key model

A

The substrate binds to the active site of the enzyme, which forms an Enzyme-Substrate complex
The Substrate leaves as 2 products after the reaction

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11
Q

Give a main difference between the Induced fit model and the lock and key model

A

In the Lock and Key model, the Substrate fits exactly to the Enzymes active site
In the Induced fit model, the Enzyme moulds itself around the substrate

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12
Q

Of the 2 models of Enzyme action which is more useful and why

A

Induced-fit model as it better explains the way in which activation energy is lower in catabolic reactions

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13
Q

How does an increase in Substrate concentration effect Enzyme activity

A

As you increase the substrate concentration, enzyme activity increases, as there is a higher chance of collisions meaning more Enzyme substrate complexes

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14
Q

What happens to Enzyme activity when Substrate concentration bypasses the Enzyme concentration

A

Enzyme activity does not increase, as all the active sites have been taken up by Substrates

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15
Q

How does an increase in Enzyme concentration effect Enzyme activity

A

An increase in enzyme concentration increases the rate of reaction, as there is more Enzyme substrate complexes formed

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16
Q

Why may a enzyme concentration graph level off at high Enzyme concentrations

A

There is insufficient substrate

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17
Q

How does a change to the optimum pH effect Enzyme activity

A

It will decrease Enzyme activity as the active sites of the enzymes are altered by changes in pH

18
Q

Past the optimum pH, what happens to the bonds inside an enzyme

A

Ionic bonds in the tertiary structure of a protein will be disrupted

19
Q

What is pH

A

A measure of hydrogen ion concentration

20
Q

How does an increase in temperature effect Enzyme activity

A

It causes an exponential increase in Enzyme activity. This is due to the increase in temperature providing more kinetic energy for more collisions between Enzymes and substrates

21
Q

What happens to the Enzyme past the Optimum temperature

A

The bonds that hold the tertiary structure of the enzyme molecules are broken and so the active site loses its complementary shape

22
Q

What is a Co-factor

A

An enzyme with a non-protein part attached

23
Q

What is a coenzyme

A

An organic molecule that are often derivatives of vitamins

24
Q

How do Cofactors function

A

They either influence the shape of an enzyme or they participate in the enzymatic reaction

25
Q

What is the difference between Competitive and Non-Competitive Inhibition

A

Competitive inhibitors closely resemble the structure of the substrate and so competes for the active site
Nom-competitive inhibitors don’t resemble the substrate and so bind to a part of the enzyme away from the active site

26
Q

Of the 2 inhibitors, which of them changes the shape of the Enzyme permanently

A

Non-competitive inhibitors

27
Q

Out of the Enzyme not having an inhibitor, competitive inhibitor and a non-competitive inhibitor, which increases the Enzyme activity the most

A

The enzyme with no inhibitor

28
Q

What is the effect of a competitive inhibitor

A

If there is a high substrate concentration, the effect of the inhibitor is reduced

29
Q

What is the effect of a non-competitive inhibitor

A

As the inhibitor is not competing for the active site, an increase in substrate concentration will have no effect on the inhibitor

30
Q

What is Adsorption

A

The enzymes are attached by weak forces to an inert substance such as glass or a matrix

31
Q

What is entrapment

A

The enzymes are trapped within polymers such as Alginate beads or microspheres

32
Q

What is Encapsulation

A

The enzymes are trapped inside a selectively permeable membrane such as Nylon

33
Q

What is Cross-Linkage

A

The enzymes are bonded covalently to a matrix, such as cellulose, as a sequence of chemical reactions

34
Q

What are some commercial advantages of Enzyme immobilisation

A

Production can take place continuously
The product is enzyme-free, so purification costs are reduced
The enzyme remains separate from the reaction mixture
The enzymes stability is improved, meaning it remains active over a greater range of pH and temperatures

35
Q

What are some advantages and disadvantages of Adsorption as a method of Enzyme immobilisation

A

Advantages - Easy to Immobilise and so relatively cheap

Disadvantages- Enzymes can be washed away ; some active sites may be blocked by the absorptive material

36
Q

What are some advantages and disadvantages of Cross-Linking as a method of Enzyme immobilisation

A

Advantages- enzymes securely bonded, so not washed away; resistant to pH and temperature changes
Disadvantages- Active sites may be blocked by binding chemicals; significant distortion of some active sites during binding process

37
Q

What are some advantages and disadvantages of Encapsulation as a method of Enzyme immobilisation

A

Advantages- Enzymes not bound, so active sites are not blocked and activity is not adversely affected
Disadvantages - Substrate has to diffuse through mesh; some enzymes may leak out through mesh

38
Q

What are some advantages and disadvantages of Entrapment as a method of Enzyme immobilisation

A

Advantages - Enzymes cannot leak out; since enzymes not bound, active sites are not blocked
Disadvantages - Resistance to substrates diffusing into a gel matrix and products diffusing out

39
Q

How do Biosensors use immobilised enzymes

A

To detect or monitor a particular molecule

40
Q

What do glucose test strips utilise and what do they do

A

They utilise the enzyme glucose oxidase, which specifically acts on glucose in the presence of oxygen to yield glauconite acid and hydrogen peroxide