Syllabus Edition

First teaching 2023

First exams 2025

|

Vmax & the Michaelis-Menten Constant (CIE AS Biology)

Revision Note

Cara Head

Author

Cara Head

Last updated

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 and 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) and 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), which is 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) and 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

Michaelis-Menten Model  Diagram

Graph showing the Michaelis-Menten model, downloadable AS & A Level Biology revision notes

A graph showing the effect of substrate concentration on initial reaction rate, with Vmax, ½Vmax and Km values shown

Examiner Tip

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

You've read 0 of your 5 free revision notes this week

Sign up now. It’s free!

Join the 100,000+ Students that ❤️ Save My Exams

the (exam) results speak for themselves:

Did this page help you?

Cara Head

Author: Cara Head

Expertise: Biology

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