Carboxylesterases: General detoxifying enzymes

Chem Biol Interact. 2016 Nov 25;259(Pt B):327-331. doi: 10.1016/j.cbi.2016.02.011. Epub 2016 Feb 15.


Carboxylesterases (CE) are members of the esterase family of enzymes, and as their name suggests, they are responsible for the hydrolysis of carboxylesters into the corresponding alcohol and carboxylic acid. To date, no endogenous CE substrates have been identified and as such, these proteins are thought to act as a mechanism to detoxify ester-containing xenobiotics. As a consequence, they are expressed in tissues that might be exposed to such agents (lung and gut epithelia, liver, kidney, etc.). CEs demonstrate very broad substrate specificities and can hydrolyze compounds as diverse as cocaine, oseltamivir (Tamiflu), permethrin and irinotecan. In addition, these enzymes are irreversibly inhibited by organophosphates such as Sarin and Tabun. In this overview, we will compare and contrast the two human enzymes that have been characterized, and evaluate the biology of the interaction of these proteins with organophosphates (principally nerve agents).

Keywords: Carboxylesterase; Expression; Hydrolysis; Organophosphorus compounds; Structure.

Publication types

  • Review

MeSH terms

  • Animals
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / metabolism*
  • Humans
  • Inactivation, Metabolic
  • Models, Molecular
  • Organophosphates / metabolism
  • Substrate Specificity


  • Organophosphates
  • Carboxylic Ester Hydrolases