3. Enzymes Flashcards

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1
Q

What is an enzyme?

A

a protein biological catalyst, that speeds up chemical reactions by lowering the activation energy of reactions.

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2
Q

Draw a 3-part enzyme diagram.

A
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3
Q

Explain what determines the structure of the active site.

A

Because the enzyme (protein) is made from a sequence of amino acids then the R groups from these determine the bonds that will form. Therefore leading to the overall 3D structure, including the active site.

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4
Q

Define metabolism

A

The sum total of all chemical reactions occurring in an organism

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5
Q

What does a synthesis reaction mean?

A

Two substrates combine to form one product

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6
Q

What does a decomposition reaction mean?

A

One substrate breaks down to form two products

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7
Q

What factors affect the rate of enzyme reactions?

A

Temperature
pH
Enzyme concentration
Substrate concentration
Competitive inhibitors
Non-competitive inhibitors

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8
Q

Draw an enzyme Rate of reaction vs temperature graph

A
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9
Q

Explain why the enzyme controlled reaction is low at a low temperature

A

Because the enzymes are inactive
Then there is less kinetic energy and it is less likely to have successful collisions between enzymes and substrate
Therefore less enzyme-substrate complexes will form, less products will form and there is a lower rate of reaction

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10
Q

Define optimum temperature

A

Temperature where the enzyme works best and there is the most enzyme substrate complexes forming.

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11
Q

Explain why the enzyme controlled reaction is low at a high temperature

A

Because there is too much kinetic energy the enzyme’s denature
Then the 3D structure of the active site has changed shape so it is no longer specific and complementary to the substrate
Therefore less enzyme-substrate complexes will form and there will be less products and a lower rate of reaction.

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12
Q

Draw an enzyme Rate of reaction reaction vs pH graph

A
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13
Q

Explain why the enzyme controlled reaction is low at a low pH

A

Because the pH is too low the enzyme’s denature
Then the 3D structure of the active site has changed shape so it is no longer specific and complementary to the substrate.
Therefore less enzyme-substrate complexes will form and there will be less products formed and a lower rate of reaction.

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14
Q

Explain why the enzyme controlled reaction is low at a high pH

A

Because the pH is too high the enzyme’s denature
Then the 3D structure of the active site has changed shape so it is no longer specific and complementary to the substrate.
Therefore less enzyme-substrate complexes will form and there is less products and a lower rate of reaction.

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15
Q

Draw an enzyme rate of reaction vs enzyme concentration (assuming unlimited substrate concentration)

A
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16
Q

Draw an enzyme rate of reaction vs substrate concentration graph

A
17
Q

What is a competitive inhibitor?

A

Competitive inhibitors are specific and complimentary to the active site of the enzyme, they bind to the active site instead of the substrate. Therefore less enzyme-substrate complexes form.

18
Q

What is a non-competitive inhibitor?

A

Non-competitive binds to the allosteric site (not the active site) and causes a shape change. The 3D structure of the active site changes shape so that it is no longer specific and complimentary to the substrate. Therefore less enzyme-substrate complexes form.

19
Q

Draw a 3-part enzyme diagram showing competitive inhibition

A

Remember to always draw the normal 3-part enzyme diagram first.

20
Q

Draw a 3-part enzyme diagram showing non-competitive inhibition

A
21
Q

How can the rate of reaction be increased in the presence of a competitive inhibitor?

A

Increase substrate concentration

22
Q

What is an enzyme-substrate complex?

A

When the enzyme and substrate have successfully collided and bound together

23
Q

What factors cause an enzyme to denature?

A

High temperatures (above the optimum), high or low pH (above or below the optimum)

24
Q

Why does the graph plateau in an enzyme rate of reaction vs substrate concentration graph?

A

Because all enzyme active sites are occupied with substrate
Then the maximum number of enzyme substrate complexes are already forming each second
Therefore the reaction rate plateaus and cannot increase regardless of an increase in substrate.