The origins of enzyme kinetics

FEBS Lett. 2013 Sep 2;587(17):2725-30. doi: 10.1016/j.febslet.2013.06.009. Epub 2013 Jun 19.

Abstract

The equation commonly called the Michaelis-Menten equation is sometimes attributed to other authors. However, although Victor Henri had derived the equation from the correct mechanism, and Adrian Brown before him had proposed the idea of enzyme saturation, it was Leonor Michaelis and Maud Menten who showed that this mechanism could also be deduced on the basis of an experimental approach that paid proper attention to pH and spontaneous changes in the product after formation in the enzyme-catalysed reaction. By using initial rates of reaction they avoided the complications due to substrate depletion, product accumulation and progressive inactivation of the enzyme that had made attempts to analyse complete time courses very difficult. Their methodology has remained the standard approach to steady-state enzyme kinetics ever since.

Keywords: Henri; Kinetics; Menten; Michaelis; Steady state.

Publication types

  • Historical Article
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Algorithms*
  • Biocatalysis
  • Biochemistry / history*
  • Enzyme Inhibitors / chemistry
  • Enzymes / chemistry
  • History, 20th Century
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics

Substances

  • Enzyme Inhibitors
  • Enzymes