Biology · University
Enzyme kinetics and biological rate models · revision notes
Enzymes catalyse reactions without being consumed in the net reaction. They alter rates but not the equilibrium constant for a given reaction and conditions.
Key ideas and conditions
Catalysis
Enzymes catalyse reactions without being consumed in the net reaction. They alter rates but not the equilibrium constant for a given reaction and conditions.
Saturation
The Michaelis-Menten model gives v=Vmax[S]/(Km+[S]) under its assumptions. Saturation arises when increasing substrate gives diminishing rate increases.
Parameters
At [S]=Km, the model rate is Vmax/2. Km is not universally equal to a dissociation constant or a direct affinity measure in every mechanism.
Data
Estimate kinetic parameters from appropriate data with uncertainty. A fitted curve does not establish that every mechanistic assumption is true.
Explain without looking
- At [S]=0 in the simple stated model with positive Km, find v.
- Why should parameter estimates include uncertainty rather than only a fitted best value?
Further reading and review references
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