Syllabus Edition

First teaching 2020

Last exams 2024

|

Vmax & the Michaelis-Menten Constant (CIE A Level Biology)

Revision Note

Test yourself
Lára

Author

Lára

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 (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 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!

You've read 0 of your 10 free revision notes

Unlock more, it's free!

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

the (exam) results speak for themselves:

Did this page help you?

Lára

Author: Lára

Expertise: Biology Lead

Lára graduated from Oxford University in Biological Sciences and has now been a science tutor working in the UK for several years. Lára has a particular interest in the area of infectious disease and epidemiology, and enjoys creating original educational materials that develop confidence and facilitate learning.