Biological Molecules: Many proteins are enzymes Flashcards

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1
Q

How do enzymes work to speed up a reaction?

A

They lower the activation energy required to start a reaction

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2
Q

What determines the shape of an enzyme’s active site?

A

Its tertiary structure

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3
Q

Explain the induced fit model:

A
  • Enzyme’s active site and substrate have a similar shape but are not completely complementary
  • When the substrate starts to bind, the active site changes shape to become complementary
  • This puts stress on the substrates bonds making them easier to break, lowering the activation energy
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4
Q

How does an increasing enzyme concentration impact the rate of reaction if there are excess substrates?

A
  • Increase reaction (linear)
  • There will be more active sites and sufficient substrates
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5
Q

How does an increasing enzyme concentration impact the rate of reaction if there is limited substrates?

A
  • Increase reaction partially then level off
  • There will be more active sites (increase at the start)
  • But then an insufficient amount of substrate (level off)
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6
Q

How does an increasing substrate concentration impact the rate of reaction if there are excess enzymes?

A
  • Increase reaction (linear)
  • There will be more substrates and sufficient enzymes
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7
Q

How does an increasing substrate concentration impact the rate of reaction if there are limited enzymes?

A
  • Increase reaction partially then level off
  • There will be more substrates (increase at the start)
  • But then an insufficient amount of enzymes (level off)
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8
Q

How do competitive inhibitors impact the rate of reaction if there are an increasing number of substrates?

A
  • Initial decrease (Competitive inhibitor binds to enzyme and so prevents other substrate molecules from doing so)
  • Maximum rate of reaction is reached (competitive inhibitors only temporarily bind to the enzyme)
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9
Q

How do non-competitive inhibitors impact the rate of reaction if there are an increasing number of substrates?

A
  • Decreases (maximum) rate of reaction
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10
Q

How does temperature affect rate of reaction?

A
  • Increase up to optimum temperature
  • Rapid decrease after optimum temperature
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11
Q

How do high temperatures after the optimum temperature slow down enzymes and the rate of reaction?

A
  • Break hydrogen bonds
  • Changes tertiary structure
  • Changes active site
  • Reduces frequency of enzyme-substrate complex forming
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12
Q

How do changes in pH slow down enzymes and the rate of reaction?

A
  • Breaks hydrogen and ionic bonds
  • Changes tertiary structure
  • Changes active site
  • Reduces frequency of enzyme-substrate complex forming
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13
Q

How do enzymes speed up the rate of chemical reactions?

A

Lower the activation energy needed for the reaction to start.

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14
Q

Give the two reasons why forming an enzyme-substrate complex lowers the activation energy:

A

1) The enzyme will hold two substrate molecules together, reducing repulsion so they can bond more easily.
2) Enzymes put strain on the substrates bonds when catalysing, so the substrate breaks up more easily.

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15
Q

What are the two enzyme models?

A
  • Lock and key model
  • Induced fit model
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16
Q

Explain the process of the lock and key model:

A
  • Enzyme and substrate fit like a ‘lock and key’
  • Substrate and active site have a complementary shape
17
Q

Why is the lock and key model not a full explanation?

A

Evidence shows that the enzyme-substrate complex changes shape slightly to complete the fit.

17
Q

Explain the process of the induced fit model:

A
  • Substrate binds to enzymes active site
  • Enzymes active site changes slightly so enzyme-substrate complex is completed.
18
Q

Why are enzymes only able to catalyse one specific substrate?

A

Only one complementary substrate will fit into the active site.

19
Q

An enzymes active site is determined by its ________.

A

Tertiary structure

20
Q

An enzymes tertiary structure is determined by its _______.

A

Primary structure.

21
Q

What determines an enzymes primary structure?

A

Genes

22
Q

What are the two ways of measuring the rate of a reaction?

A

1) Measuring how fast a product is made.
2) Measuring how fast a substrate is broken down.

23
Q

How does pH affect rate of reaction?

A
  • Increase up to optimum pH
  • Rapid decrease after optimum pH
24
Q

What are enzyme inhibitors?

A

Molecules that bind to an enzyme and inhibit a reaction.

25
Q

Inhibition can either be _______ or ________.

A

Competitive or non-competitive.

26
Q

What do competitive inhibitors do?

A

Compete with substrate molecules to bind to the enzymes active site.

27
Q

Competitive inhibitors have a _______ shape to that of substrate molecules.

A

Similar

28
Q

When competitive inhibitors bind to an enzyme, a reaction ____ take place.

A

Doesn’t

29
Q

What do non-competitive inhibitors do?

A

Bind to the enzyme away from its active site, causing the active site to change shape so its complementary substrate can no longer fit.

30
Q

What are the two types of enzyme inhibitors?

A

Competitive
Non-competitive