Michaelis-Menten Kinetics

Biochemical Engineering

The following is known as Michaelis-Menten reaction kinetics. 

           k1         k2
  E + S <------> ES ------> E + P
           k-1
Derive Michaelis-Menten reaction rate expression with different assumptions.
  1. Equilibrium Assumption
  2. Sequential irrevesible Reaction Assumption
  3. Quasi-Steady State Assumption

Derivation of Michaelis-Menten Rate Expression

It is clear from the above file that many assumptions lead to the same saturation form.

To find how the substrate or product concentration changes with time, we integrate the Michaelis-Menten rate expression symbolically.

The following files deal with the case where the second step is reversible, which leads to product inhibition. 
           k1          k2
  E + S <------> ES <------> E + P
           k-1         k-2

Symbolic Derivation of Enzymatic Reaction Rate (Product Inhibition)

Furthermore, when the enzyme deactivates with time in a first-order fashion, we simply add one more equation to describe the deactivation of the enzyme, although the resulting equations become a bit more complicated. The problem becomes much more interesting.

With Enzyme Deactivation -- Temperature Effect

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Biochemical Engineering -- Michaelis-Menten Kinetics
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