Team:Imperial College London/Drylab/Enzyme/Analysis/Detailed

The behaviour of the system can be described with ODEs. The first 4 equations describe the single-substrate mechanism for an enzyme reaction without Michaelis-Menten assumptions, while equation 5 describes modification with the Michaelis-Menten assumption.

The Enzyme Mechanism

k1, k2 ,k3 are the kinetic rate constants for each step.

In substrate binding, 1 molecule of Enzyme (E) binds with 1 molecule of Substrate (S) in a reversible reaction to form the Enzyme-Substrate complex (ES). We are unable to measure this step.

In catalysis, the Enzyme-Substrate complex (ES) produces the unchanged enzyme (E) and the product (P) in an irreversible reaction. This step can be measured.

When [S] becomes high enough, the second step of the enzyme kinetics becomes the rate determining step, controlled by k3.
This enzyme mechanism scheme can be described by the following differential equations describing rate of change of each component. Each component is described by a simple rate term for either its production or its decomposition.