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).
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Hatfield MJ,Umans RA,Hyatt JL,Edwards CC,Wierdl M,Tsurkan L,Taylor MR,Potter PMdoi
10.1016/j.cbi.2016.02.011subject
Has Abstractpub_date
2016-11-25 00:00:00pages
327-331issue
Pt Beissn
0009-2797issn
1872-7786pii
S0009-2797(16)30047-3journal_volume
259pub_type
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