Enzymes Flashcards

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1
Q

Characteristics of Enzymes

A
  1. Catalyse chemical reactions
  2. Catalyse reversible reactions
  3. Sensitive to pH
  4. Sensitive to temperature
  5. Highly specific in actions
  6. Required in minute amounts
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2
Q

Describe the process of denaturation

A
  1. The 3 dimensional structure of the enzyme is changed,
  2. resulting in the loss or alteration of the active site,
  3. causing the substrate to no longer be able to fit in the enzyme’s active site.
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3
Q

How does a competitive inhibitor inhibit enzyme function?

A
  1. A competitive inhibitor is often of a similar 3 dimensional configuration to the substrate.
  2. Competitive inhibitors compete with the substrates for the active site of the enzymes
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4
Q

How can the effect of a competitive inhibitor be reduced?

A
  1. Increasing the concentration of the substrate.
  2. This increases the probability of an enzyme-substrate collision rather than an enzyme-inhibitor collision.
  3. Rate of reaction increases.
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5
Q

How does a non-competitive inhibitor inhibit enzyme function?

A
  1. A non-competitive inhibitor does not have any structural resemblance to the substrate.
  2. It combines with the enzyme in regions other than the active site.
  3. Puts a proportion of enzyme molecules out of action.
  4. Results in a change in conformation of the enzyme molecule, including the configuration of the active site.
  5. The rate of reaction with a non-competitive inhibitor can never reach its maximum, even when the substrate concentration is increased to a high level.
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6
Q

What are the differences between a competitive inhibitor and a non-competitive inhibitor?

A
  1. Structure
  2. Site of binding
  3. Effect of increasing substrate concentration.
  4. Maximum rate of reaction.
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