Michaelis–Menten Enzyme Kinetics

1D Ordinary Differential Equations

Michaelis–Menten kinetics is a foundational model in biochemical reaction dynamics. It relates substrate concentration to reaction rate using a saturating nonlinearity.

The (simplified) substrate dynamics implemented in the reference script is:

\[ \dot s = \frac{V_{\max}s}{K_m + s} \]

where \(V_{\max}\) is the maximum rate and \(K_m\) is the Michaelis constant.

Reference Implementation

See:

  • sessions/s01_odes_1d/michaelis_menten.py

The helper plot_michaelis_menten(...) produces:

  • \(s(t)\) over time
  • \(v(s)\) with guides at \(s=K_m\) and \(v=V_{\max}/2\)

Render-time Figure

Figure 1: Michaelis–Menten: time series \(s(t)\) and rate curve \(v(s)\).

Exploration

  1. Increase \(V_{\max}\) and observe how the rate curve changes.
  2. Increase \(K_m\) (lower affinity). How does the saturation point shift?

Run Locally

python sessions/s01_odes_1d/michaelis_menten.py