期刊
CHEMICO-BIOLOGICAL INTERACTIONS
卷 259, 期 -, 页码 327-331出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.cbi.2016.02.011
关键词
Carboxylesterase; Expression; Organophosphorus compounds; Structure; Hydrolysis
资金
- NCCIH NIH HHS [R01 AT007531] Funding Source: Medline
- NCI NIH HHS [R01 CA108775, R01 CA098468, P30 CA021765] Funding Source: Medline
- NIDA NIH HHS [R01 DA018116] Funding Source: Medline
- NINDS NIH HHS [U01 NS058089, U01 NS082328] Funding Source: Medline
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). (C) 2016 Elsevier Ireland Ltd. All rights reserved.
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