Topic 2- Enzymes Flashcards

(40 cards)

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
What is the difference between Competitive and Non-Competitive Inhibition
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
Of the 2 inhibitors, which of them changes the shape of the Enzyme permanently
Non-competitive inhibitors
27
Out of the Enzyme not having an inhibitor, competitive inhibitor and a non-competitive inhibitor, which increases the Enzyme activity the most
The enzyme with no inhibitor
28
What is the effect of a competitive inhibitor
If there is a high substrate concentration, the effect of the inhibitor is reduced
29
What is the effect of a non-competitive inhibitor
As the inhibitor is not competing for the active site, an increase in substrate concentration will have no effect on the inhibitor
30
What is Adsorption
The enzymes are attached by weak forces to an inert substance such as glass or a matrix
31
What is entrapment
The enzymes are trapped within polymers such as Alginate beads or microspheres
32
What is Encapsulation
The enzymes are trapped inside a selectively permeable membrane such as Nylon
33
What is Cross-Linkage
The enzymes are bonded covalently to a matrix, such as cellulose, as a sequence of chemical reactions
34
What are some commercial advantages of Enzyme immobilisation
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
What are some advantages and disadvantages of Adsorption as a method of Enzyme immobilisation
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
What are some advantages and disadvantages of Cross-Linking as a method of Enzyme immobilisation
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
What are some advantages and disadvantages of Encapsulation as a method of Enzyme immobilisation
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
What are some advantages and disadvantages of Entrapment as a method of Enzyme immobilisation
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
How do Biosensors use immobilised enzymes
To detect or monitor a particular molecule
40
What do glucose test strips utilise and what do they do
They utilise the enzyme glucose oxidase, which specifically acts on glucose in the presence of oxygen to yield glauconite acid and hydrogen peroxide