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Biology AS CIE

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  1. 1-cell-structure
    10 主题
  2. 2-biological-molecules
    19 主题
  3. 3-enzymes
    13 主题
  4. 4-cell-membranes-and-transport
    16 主题
  5. 5-the-mitotic-cell-cycle
    8 主题
  6. 6-nucleic-acids-and-protein-synthesis
    9 主题
  7. 7-transport-in-plants
    11 主题
  8. 8-transport-in-mammals
    16 主题
  9. 9-gas-exchange
    6 主题
  10. 10-infectious-diseases
    6 主题
  11. 11-immunity
    10 主题
课 3, 主题 3
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3-2-factors-that-affect-enzyme-action AS vmax-and-the-michaelis-menten-constant

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Exam code:9700

Vmax & the Michaelis-Menten constant

  • Substrate concentration affects the rate of catalysis in an enzyme-substrate reaction

    • When the substrate concentration is fixed (and enzyme concentration is kept constant) the initial rate of reaction is fastest

    • As active sites become engaged, the reaction rate falls

  • The Michaelis-Menten model describes the kinetics of such enzyme catalysed reactions

  • In this model, two values are used to describe an enzyme catalysed reaction:

    • The maximal rate or maximal velocity (Vmax)

    • The Michaelis-Menten constant (Km)

  • These values are derived from the reaction rate at different substrate concentrations

  • The maximum rate of reaction (Vmax) is used to derive the Michaelis–Menten constant (Km)

    • This is then used to compare the affinity of different enzymes for their substrates

Michaelis-Menten enzyme kinetics

  • The Michaelis-Menten model is used to investigate the kinetics of enzyme catalysed reactions (enzyme kinetics is an area in biochemistry that studies how different variables affect reaction rates)

  • The rate of reaction is measured at different substrate concentrations, producing a graph like the one below

  • The two important values deduced are:

    • The Vmax (maximum rate of reaction at saturating substrate concentrations)

    • The Km, which is the substrate concentration at ½Vmax (this is also known as the Michaelis-Menten constant)

      • The Michaelis-Menten constant is the substrate concentration at which the enzyme works at half its maximum rate

      • At this point, half of the active sites of the enzyme are occupied by substrate molecules

      • The higher the affinity of the enzyme for the substrate, the lower the substrate concentration needed for this to occur

      • This is why the Michaelis-Menten constant is a measure of the affinity of an enzyme for its substrate

  • There is an inverse relationship between the Km and the affinity of an enzyme for its substrate

  • An enzyme with a high Km has a low affinity for its substrate and an enzyme with a low Km has a high affinity for its substrate

Graph showing reaction rate vs. substrate concentration. Velocity levels off at high concentration, increases linearly at low concentration.
A graph showing the effect of substrate concentration on initial reaction rate, with Vmax, ½Vmax and Km values shown

Examiner Tips and Tricks

Make sure you can identify the Vmax and the Km on a graph like the one above. 

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