| Literature DB >> 26892220 |
M Jason Hatfield1, Robyn A Umans1, Janice L Hyatt1, Carol C Edwards1, Monika Wierdl1, Lyudmila Tsurkan1, Michael R Taylor1, Philip M Potter2.
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). Copyright ÂEntities:
Keywords: Carboxylesterase; Expression; Hydrolysis; Organophosphorus compounds; Structure
Mesh:
Substances:
Year: 2016 PMID: 26892220 PMCID: PMC4985501 DOI: 10.1016/j.cbi.2016.02.011
Source DB: PubMed Journal: Chem Biol Interact ISSN: 0009-2797 Impact factor: 5.192