BM: Factors Affecting Enzyme Action COPY Flashcards
What factors affect enzyme activity?
- Temperature
- pH
- Enzyme concentration
- Substrate concentration
Draw a graph showing how temperature affects the rate of reaction:
Draw a graph showing how pH affects enzyme action:
Draw a diagram showing how enzyme concentration affects the rate of reaction:
Describe the effect substrate concentration has on the rate of reaction:
- Higher concentration = faster reaction
- Saturation point is reached - active sites are ‘full’
- If no other variables are changed, rate will fall as substrate conc. decreases with time.
Describe the effect temperature has on enzyme-controlled reactions
- As temperature increases, the kinetic energy increases. This allows more ES (enzyme-substrate) complexes to form.
- The rate of reaction increases up to the optimum temperature
- Once past optimum temp, bonds in the tertiary structure of the enzymes break - changing the stte of the active site
Describe the effect pH has on enzyme-controlled reactions
- All enzymes have an optimum pH
- if the pH is below or exceeds the optimal pH, the H+ and OH- ions interfere with the ionic and hydrogen bonds in an enzymes tertiary structure.
- This changes its shape. It is denatured and no longer works
Describe the effect enzyme concentration has on enzyme-controlled reactions
- increasing enzyme concentration will increase rate of reaction, as more enzymes will collide with substrates
- enzyme concentration only has effect up to a certain concentration because it is no longer a limiting factor
What are the two types of inhibition?
Competitive and non-competitive
Describe competitive inhibition:
- Inhibitor molecules have similar shape to substrate molecules.
- Compete with substrate molecules to bind to active site.
- No reaction occurs, but they block active site.
What happens if there is a high concentration of inhibitor molecules relative to substrate molecules?
Inhibitor wil ltake up nearly all of active sites.
Describe non-competitive inhibition:
- Inhibitor molecules bind to allosteric site.
- Active site changes shape so substrate can no longer bind to it.
What happens if substrate concentration is increased during competitive inhibition?
Rate will increase as substrates have an increased chance of reaching active site before inhibitor.
What happens if substrate concentration is increased during non- competitive inhibition?
Reaction rate will stay the same - enxyme activity will still be inhibited.