Enzymes Flashcards

1
Q

What is an enzyme?

A

Enzymes are tertiary structure proteins that catalyse a wide range of reactions

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2
Q

What is the function of enzymes?

A

Enzymes are biological catalysts so they lower the activation energy of a reaction

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3
Q

Do enzymes get used up in reactions?

A

No

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4
Q

What is the activation energy?

A

The minimum amount of energy required for a reaction to occur

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5
Q

What part of an enzyme attaches to a substrate?

A

The active site

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6
Q

Describe the shape of an active site

A

Specific and unique due to the sequence of amino acids

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7
Q

Why is the unique shape of the active site in an enzyme important?

A

It ensures that enzymes can only bind to substrates that are complementary in shape

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8
Q

What is the induced-fit model?

A
  • Before the reaction the active site of an enzyme in not completely complementary to the substrate
  • The active site will change shape as the substrate binds, forming an enzyme-substrate complex
  • This distorts the bond in the substrate which leads to a reaction
  • Once products are formed they are released and active site returns to its original shape
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9
Q

What factors affect the rate of enzyme controlled reactions?

A
  • Temperature
  • pH
  • Substrate concentration
  • Enzyme concentration
  • Competitive inhibitors
  • Non-competitive inhibitors
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10
Q

How does temperature affect enzyme controlled reactions?

A

As temperature increases the rate of reaction will increase due to more successful collisions between the substrate and the enzyme so more enzyme-substrate complexes form

However at too high a temperature there will be too much kinetic energy and the enzyme will denature and its active site will change shape resulting in enzyme-substrate complexes no longer being able to form as the active site is no longer complementary to the substrate

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11
Q

How does pH affect enzyme controlled reactions?

A
  • Too high/too low a pH will cause the enzyme to denature and its active site will change shape
  • Enzyme-substrate complexes can no longer form as the active site is no longer complementary to the substrate
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12
Q

How does substrate concentration affect enzyme controlled reactions?

A
  • More substrate results in more successful collisions between the enzyme and the substrate
  • More enzyme-substrate complexes are formed
  • However the rate of reaction plateaus as enzyme concentration becomes the limiting factor as all active sites are saturated
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13
Q

How does enzyme concentration affect enzyme controlled reactions?

A
  • More active sites available so more successful collisions between the enzyme and the substrate
  • More enzyme-substrate complexes are formed
  • However the rate of reaction plateaus as substrate concentration becomes the limiting factor
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14
Q

How do competitive inhibitors affect enzyme controlled reactions?

A
  • They have a similar shape as the substrate and can bind to active site
  • This prevents the substrate from binding to the enzymes active site
  • If more substrate is added this will out-compete the inhibitor and knock them out of the active site
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15
Q

How do non-competitive inhibitors affect enzyme controlled reactions?

A
  • They bind to the enzyme away from the active site called the allosteric site
  • This causes the active site to change shape and the substrate can no longer bind as the active site is no longer complementary to the substrate
  • Enzyme-substrate complexes can no longer form
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