Enzyme kinetics

Cards (27)

  • What is Enzyme kinetics
    Describing how an enzyme or inhibitor works under different conditions. These include pH, substrate and enzyme concentrations, temperature.
  • What does an effective inhibitor do to the reaction rate
    Slows down the reaction
  • What is the relashionship between substrate and rate without an enzyme
    Directly proportional
  • What shape is the rate graph with an enzyme
    Rectangular hyperbola
  • What happens to the rate once the substrate concentration is high
    The rate becomes independent of substrate concentration and dependent on the formation of the enzyme-substrate complex.
  • What happens at Vmax.
    The active site is saturated
  • Define Vmax
    The maximum possible rate of the reaction at that particular enzyme concentration
  • Define Km
    The substrate concentration at half of Vmax.
  • What is the requirement to reach Vmax
    Infinate substrate
  • Assumptions and limitations of Michaelis-Menten kinetics
    • Reaction is a single substrate reaction
    • K2 is negligible
  • Which way does the curve shift if enzyme B has higher affinity than A?
    To the left as Km is lower.
  • What is the name for a double reciprocal plot
    Lineweaver-Burk plot
  • What is the equation for rate from the hyperbola graph
    V =(Vmax * [S]) / (Km + [S])
  • What does a low Km indicate
    A high affinity for the enzyme
  • What is the unit for Velocity in enzyme reactions
    nmol / min
  • What is the unit for concentration in enzyme reactions

    nmol / liter
  • What is Km independant of
    The enzyme and substrate concentrations
  • What is Vmax dependant and independant on
    Independant of substrate concentration. Dependent on enzyme concentration.
  • Describe the Michaelis-Menten assumption that the reaction involves 1 substrate
    Substrates can have different binding sites or impact the binding of another.
  • What is the assumption in this equation?
    That K2 cannot be reversed.
    It assumes that there is no reverse catalysis or product inhibition.
    A) K1
    B) K2
    C) K-1
  • How is a Michaelis-Menten graph created
    • Measure product formation over time at different substrate concentrations
    • Plot Initial velocity [Vo]
  • What is the equation for turnover number
    Kcat = Vmax / [Et]. Where Et = [E] + [ES].
  • What is used to compare the efficiency of unrelated enzymes
    Kcat.
  • What are the features of the Lineweaver-Bruk plot
    When you plot the reciprocal values for rate and concentration, it produces a linear graph.
  • What are the two intercepts of a Lineweaver-Burk plot
    -1/Km. And 1/Vmax.
  • What is the relashionship between [S] and rate at low concentration of [S]
    Proportional
  • What is the relashionship between rate and [S]
    Proportional