Estimating kinetic constants in the Michaelis-Menten model from one enzymatic assay using Approximate Bayesian Computation

FEBS Lett. 2019 Oct;593(19):2742-2750. doi: 10.1002/1873-3468.13531. Epub 2019 Jul 21.

Abstract

The Michaelis-Menten equation is one of the most extensively used models in biochemistry for studying enzyme kinetics. However, this model requires at least a couple (e.g., eight or more) of measurements at different substrate concentrations to determine kinetic parameters. Here, we report the discovery of a novel tool for calculating kinetic constants in the Michaelis-Menten equation from only a single enzymatic assay. As a consequence, our method leads to reduced costs and time, primarily by lowering the amount of enzymes, since their isolation, storage and usage can be challenging when conducting research.

Keywords: Approximate Bayesian Computation; Bayesian statistics; Michaelis-Menten kinetics; enzymology; likelihood-free.

Publication types

  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Aminopeptidases / metabolism*
  • Animals
  • Bayes Theorem
  • Enzyme Assays / methods*
  • Enzyme Assays / standards
  • Kinetics
  • Sus scrofa

Substances

  • Aminopeptidases