Factors affecting enzyme activity

Cards (27)

  • Factors that affect enzyme activity:
    • Temperature
    • pH
    • Substrate and enzyme concentration
  • Increasing temperature:
    Kinetic energy of particles increased as they move faster and collide more often - Rate of reaction increased
  • Temperature coefficient - Q10:
    Measure of how much that rate of reaction INCREASES with a 10 degrees Celsius rise in temperature
  • Temperature coefficient:
    Rate of reaction doubles with a 10 degrees Celsius temperature increase
  • Denaturation from temperature:
    1. Higher temperatures - Bonds vibrate more
    2. Vibrations increase until bonds are strained then break
    3. Specific 3d tertiary structure changes
    4. Enzyme denatured
  • Denatured enzymes:
    1. Active site begins to change shape
    2. No longer complementary to substrate
    3. Substrate can no longer fit into active site and does not function as a catalyst
  • Optimum temperature - Temperature enzymes have the highest rate of activity
  • Most enzymes optimum is around 40 degrees Celsius
  • Change in pH = Change in hydrogen ion concentration
  • Specific 3d tertiary structure held in place by hydrogen and ionic bonds between R-groups
  • Ionic and hydrogen bonds are from interactions between polar and charged r-groups on amino acids - Primary structure formed
  • More hydrogen ions = Low pH (Acidic)
  • Fewer hydrogen ions = High pH (Alkaline)
  • Optimum pH - Active site at the right shape at a certain hydrogen ion concentration
  • Renaturation - pH changing back after optimum is surpassed and its active site is altered then returning back to normal shape
  • Denatured = When pH has a more significant change - Structure of the enzymes is irreversibly altered and active site is no longer complementary to substrate
  • Enzyme denatured - Rate of reaction is reduced
  • Changing concentration of hydrogen ions - Changes interactions hydrogen ions have with polar and charged R-groups
  • Interactions of R-groups together - Affected by interaction of R-groups with hydrogen ions
  • More hydrogen ions present (Low pH) or Less hydrogen ions present (High pH):
    1. Less the R-groups are able to interact with each other
    2. Bonds break
    3. Enzyme shape changes
  • Shape of enzymes changes as pH changes - Only functions within a narrow range
  • Increasing substrate concentration:
    1. Higher collision rate - More enzyme-substrate complexes formed
    2. Rate of reaction increases
  • Increasing concentration of enzymes:
    1. Number of available active sites increased
    2. More enzyme-substrate complexes are formed at a faster rate
  • Rate of reaction increases until Vmax
  • At Vmax:
    1. All active sites are occupied by substrate particles
    2. No more enzyme-substrate complexes can be formed until products are released from active sites
  • Increase rate of reaction past Vmax - Add more enzymes or increase temperature
  • Adding more enzymes past Vmax:
    1. More active sites are available
    2. Rate of reaction rises towards a higher Vmax
    3. Concentration of substrate becomes the limiting factor again - If increased rate of reaction rises until the higher Vmax is reached