Enzymes Flashcards
1
Q
Characteristics of Enzymes
A
- Catalyse chemical reactions
- Catalyse reversible reactions
- Sensitive to pH
- Sensitive to temperature
- Highly specific in actions
- Required in minute amounts
2
Q
Describe the process of denaturation
A
- The 3 dimensional structure of the enzyme is changed,
- resulting in the loss or alteration of the active site,
- causing the substrate to no longer be able to fit in the enzyme’s active site.
3
Q
How does a competitive inhibitor inhibit enzyme function?
A
- A competitive inhibitor is often of a similar 3 dimensional configuration to the substrate.
- Competitive inhibitors compete with the substrates for the active site of the enzymes
4
Q
How can the effect of a competitive inhibitor be reduced?
A
- Increasing the concentration of the substrate.
- This increases the probability of an enzyme-substrate collision rather than an enzyme-inhibitor collision.
- Rate of reaction increases.
5
Q
How does a non-competitive inhibitor inhibit enzyme function?
A
- A non-competitive inhibitor does not have any structural resemblance to the substrate.
- It combines with the enzyme in regions other than the active site.
- Puts a proportion of enzyme molecules out of action.
- Results in a change in conformation of the enzyme molecule, including the configuration of the active site.
- 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.
6
Q
What are the differences between a competitive inhibitor and a non-competitive inhibitor?
A
- Structure
- Site of binding
- Effect of increasing substrate concentration.
- Maximum rate of reaction.