# Michaelis-Menten Enzyme Kinetics and the Steady-State Approximation

Requires a Wolfram Notebook System

Interact on desktop, mobile and cloud with the free Wolfram Player or other Wolfram Language products.

Michaelis–Menten enzyme kinetics is a model for rate equations that has a closed-form solution for the concentrations of reactants and products in an enzymatic reaction. Certain assumptions must be made to simplify the rate equations. In particular, the steady-state approximation assumes a negligible rate of change in the concentration of the enzyme-substrate complex during the course of the reaction. Furthermore, the Michaelis–Menten reaction mechanism presupposes that catalysis is irreversible and that the enzyme is not subject to any product inhibition.

[more]
Contributed by: Brian M. Frezza (March 2011)

Open content licensed under CC BY-NC-SA

## Snapshots

## Details

Units are not explicitly given since this simulation assumes that the parameters are in coherent units. Thus if seconds were chosen in the rate constants, for example, seconds would be the unit of time throughout, and so on.

Numerical solutions were obtained using *Mathematica*'s built-in NDSolve function and closed-form solutions for the steady-state approximation were obtained from:

H. Metiu, *Physical Chemistry: Kinetics*, New York: Taylor & Francis Group, 2006.

The author of this Demonstration is a doctoral candidate at The Scripps Research Institute in La Jolla, CA, with thesis adviser M. Reza Ghadiri.