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Updated: Dec 11 2021

Enzyme Kinetics

Images free energy.jpg
  • Overview
    • Kinetic theory
      • for two molecules to react
        • they must be within bond-forming distance
        • possess enough kinetic energy to overcome the activation energy (Ea)
      • factors that affect these two conditions will either decrease or increase the reaction rate
        • temperature: causes an increase in kinetic energy
        • concentration of reactants: increases probability of collisions
    • Gibbs free energy change (ΔG)
      • is the free energy change between the products and the reactants
      • reflects the direction of a reaction and amount of reactants and products at equilibrium, but does NOT determine the rates of reaction
        • ΔG < 0: reaction is spontaneous and favors product formation
        • ΔG = 0: reaction is at equilibrium and proceeds in both direction at equal rates
        • ΔG > 0: reaction is nonspontaneous and favors reactant formation
      • Ea determines the rate of the reaction
        • a large Ea will have a slower rate
        • a small Ea will have a faster rate
      • enzymes lower the Ea allowing the reaction to proceed at a faster rate
        • enzymes do NOT change the ΔG of the reaction just the Ea
        • enzymes are sensitive to temperature and pH
  • Enzymes Kinetics
    • Michaelis-Menten Equation
      • an equation that relates the initial reaction velocity (Vi) to the substrate concentration
        • Vmax is directly proportional to the [E]
        • Km is the Michaelis-Menten constant which represents the substrate concentration at which Vi is half the maximum velocity (Vmax)
          • Km = [S] at 1/2 Vmax
          • Km is related to the enzyme's affinity for the substrate [S]
            • ↑ Km = ↓ affinity
            • ↓ Km = ↑ affinity
        • inhibitors affect these enzyme parameters
          • competitive increases Km
          • noncompetitive decreases Vmax
    • Lineweaver-Burk Equation
      • an inverted form of the Michaelis-Menten equation
        • used to calculate Vmax and Km from experimental data at below enzyme saturation levels
        • the equation is in the format y = ax + b (a is the slope and b is the y intercept)
          • y = 1/Vi
          • x = 1/[S]
          • a = Km/Vmax
          • b = 1/Vmax
        • helpful hints
          • the smaller value of -1/Km, the greater the Km
          • ↑ y-intercept = ↓ Vmax
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