1. Academic Validation
  2. Carboxylesterases: General detoxifying enzymes

Carboxylesterases: General detoxifying enzymes

  • Chem Biol Interact. 2016 Nov 25;259(Pt B):327-331. doi: 10.1016/j.cbi.2016.02.011.
M Jason Hatfield 1 Robyn A Umans 1 Janice L Hyatt 1 Carol C Edwards 1 Monika Wierdl 1 Lyudmila Tsurkan 1 Michael R Taylor 1 Philip M Potter 2
Affiliations

Affiliations

  • 1 Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
  • 2 Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN 38105, United States. Electronic address: phil.potter@stjude.org.
Abstract

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.

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