Vmax & the Michaelis-Menten Constant (Cambridge (CIE) A Level Biology): Revision Note

Exam code: 9700

Cara Head

Written by: Cara Head

Reviewed by: Alistair Marjot

Updated on

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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Cara Head

Author: Cara Head

Expertise: Biology & Psychology Content Creator

Cara graduated from the University of Exeter in 2005 with a degree in Biological Sciences. She has fifteen years of experience teaching the Sciences at KS3 to KS5, and Psychology at A-Level. Cara has taught in a range of secondary schools across the South West of England before joining the team at SME. Cara is passionate about Biology and creating resources that bring the subject alive and deepen students' understanding

Alistair Marjot

Reviewer: Alistair Marjot

Expertise: Environmental Systems and Societies & Biology Content Creator

Alistair graduated from Oxford University with a degree in Biological Sciences. He has taught GCSE/IGCSE Biology, as well as Biology and Environmental Systems & Societies for the International Baccalaureate Diploma Programme. While teaching in Oxford, Alistair completed his MA Education as Head of Department for Environmental Systems & Societies. Alistair has continued to pursue his interests in ecology and environmental science, recently gaining an MSc in Wildlife Biology & Conservation with Edinburgh Napier University.