Factors Affecting Enzyme Activity
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Questions and Answers

What is the effect of increasing substrate concentration on the velocity of the reaction?

  • It remains constant
  • It decreases
  • It increases initially, then becomes hyperbolic in shape (correct)
  • It becomes zero order kinetics
  • What is the significance of Km value in enzyme kinetics?

  • It is the substrate concentration at which 50% of enzyme molecules are bound with substrate molecules (correct)
  • It is the substrate concentration at which the reaction rate is highest
  • It is the maximum velocity of the reaction
  • It is the enzyme concentration at which the reaction rate is lowest
  • What happens to the Vmax when the enzyme concentration is doubled?

  • It becomes zero order kinetics
  • It remains the same
  • It decreases to half
  • It increases to double (correct)
  • What is the relationship between the rate of a reaction and the enzyme concentration?

    <p>The rate of the reaction is directly proportional to the enzyme concentration</p> Signup and view all the answers

    What is the shape of the reaction curve at relatively low concentrations of substrate?

    <p>Linear</p> Signup and view all the answers

    What is the effect of increasing substrate concentration on the kinetics of the reaction at first?

    <p>It becomes first order kinetics</p> Signup and view all the answers

    What is the significance of Km value in terms of enzyme concentration?

    <p>It is independent of enzyme concentration</p> Signup and view all the answers

    What is the term used to describe the plateau that appears at high substrate concentrations?

    <p>Maximum velocity</p> Signup and view all the answers

    What is the effect of increasing the concentration of enzyme on the velocity of reaction, assuming unlimited substrate concentration?

    <p>It increases the velocity of reaction proportionately</p> Signup and view all the answers

    What is the temperature at which the maximum amount of substrate is converted to the product per unit time?

    <p>The optimum temperature</p> Signup and view all the answers

    What happens to the activity of an enzyme when the temperature is increased beyond 50°C?

    <p>It decreases due to heat denaturation</p> Signup and view all the answers

    Why does the velocity of enzyme reaction decrease on both sides of the optimum pH?

    <p>Because the charge on the amino acid residues at the active site affects substrate binding and catalytic activity</p> Signup and view all the answers

    What is the typical pH range for optimum enzyme activity in humans?

    <p>Between 6 and 8</p> Signup and view all the answers

    What happens to the reaction rate in a reversible reaction when the product concentration is increased?

    <p>It slows down or stops</p> Signup and view all the answers

    What is the effect of increasing the concentration of products on the velocity of enzyme reaction?

    <p>It slows down or stops the reaction</p> Signup and view all the answers

    What is the consequence of an enzyme being blocked in a metabolic pathway?

    <p>The product accumulates and inhibits the previous enzyme</p> Signup and view all the answers

    What is the result of competitive inhibition on the Km of an enzyme?

    <p>It increases the Km.</p> Signup and view all the answers

    What type of inhibition is usually reversible?

    <p>Competitive inhibition.</p> Signup and view all the answers

    What is the effect of a non-competitive inhibitor on the Vmax of an enzyme?

    <p>It decreases the Vmax.</p> Signup and view all the answers

    What is the purpose of sulfonamides as antibacterial agents?

    <p>To inhibit the synthesis of folic acid in bacteria.</p> Signup and view all the answers

    What is the binding site for a non-competitive inhibitor on an enzyme?

    <p>A different domain on the enzyme.</p> Signup and view all the answers

    What is the result of increasing the substrate concentration in the presence of a competitive inhibitor?

    <p>The inhibition is reduced.</p> Signup and view all the answers

    What is the effect of a competitive inhibitor on the enzyme-substrate complex formation?

    <p>It decreases the formation of the enzyme-substrate complex.</p> Signup and view all the answers

    What is the purpose of calcium ions in enzyme activation?

    <p>To activate lipase.</p> Signup and view all the answers

    Study Notes

    Factors Affecting Enzyme Activity

    • Substrate concentration:
      • Velocity of reaction increases with increasing substrate concentration, initially in a linear relationship, then becoming hyperbolic
      • Km (Michaelis constant) is the substrate concentration at half-maximal velocity, representing 50% of enzyme molecules bound to substrate
      • Km is independent of enzyme concentration and remains constant for an enzyme
    • Enzyme concentration:
      • Velocity of reaction increases proportionally with enzyme concentration when sufficient substrate is present
    • Temperature:
      • Velocity of reaction increases with temperature, reaching a maximum (optimum temperature) and then decreasing
      • Most human enzymes have an optimum temperature around 37°C
    • pH:
      • Each enzyme has an optimum pH, with velocity drastically reduced on either side of the optimum
      • pH affects the charge on amino acid residues at the active site, influencing substrate binding and catalytic activity
    • Concentration of products:
      • In reversible reactions, increased product concentration slows down the reaction rate
    • Enzyme activation:
      • Certain inorganic ions (e.g., chloride and calcium) can activate enzymes

    Enzyme Inhibition

    • Competitive inhibition:
      • Inhibitor molecules compete with substrate molecules for the active site, reducing available enzyme molecules
      • Reversible, with excess substrate abolishing the inhibition
      • Increases Km for the substrate, but does not affect Vmax
    • Non-competitive inhibition:
      • Inhibitor binds to a different domain on the enzyme, reducing enzyme activity
      • Irreversible, with no competition between substrate and inhibitor
      • Does not affect Km, but decreases Vmax

    Pharmacological Applications

    • Competitive inhibitors can be used as pharmacological agents, such as sulfonamides, which inhibit folic acid synthesis in bacteria by competing with PABA

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    Learn about the factors that influence enzyme activity, including substrate concentration and enzyme concentration, and how they impact reaction velocity.

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