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
    See similar decks