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Carboxylesterases: General detoxifying enzymes.

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).

SUBMITTER: Hatfield MJ

PROVIDER: S-EPMC4985501 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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Carboxylesterases: General detoxifying enzymes.

Hatfield M Jason MJ Umans Robyn A RA Hyatt Janice L JL Edwards Carol C CC Wierdl Monika M Tsurkan Lyudmila L Taylor Michael R MR Potter Philip M PM

Chemico-biological interactions 20160215 Pt B

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.) ...[more]

PMID: 26892220

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Project description:This study aimed to elucidate the way in which larvae of the lamprey Geotria australis counteract the potential problems of the very high concentrations of non-haem iron they contain and thereby avoid the deleterious effects associated with iron overload in other vertebrates. Particular attention has been paid to ascertaining whether increasing concentrations of iron are accompanied by (i) change to a less readily available form of iron and (ii) an increase in the activity of those detoxifying enzymes responsible for minimizing the production of harmful hydroxyl radicals via the Haber-Weiss reaction. The mean concentrations of haemosiderin and ferritin in larval G. australis were each far higher in the nephric fold than in either the liver or intestine, but all these concentrations were much greater than those in rat liver. Since haemosiderin releases iron far more slowly than ferritin, the iron it contains is much less readily available to catalyse the Haber-Weiss reaction. It is thus relevant that (i) non-haem iron in the nephric fold occurred to a greater extent as large dense haemosiderin granules than as ferritin molecules and (ii) the proportion of iron in the form of haemosiderin rose with increasing concentration of total non-haem iron. A strong correlation was also recorded between the activity of superoxide dismutase in the nephric fold and the concentrations of total non-haem iron and its haemosiderin and ferritin components. This demonstrates that enzyme detoxification of O2.- rises with increasing amounts of iron. The exceptional iron concentrations in the nephric fold were not reflected by a greater measured activity of superoxide dismutase than that found in other tissues. However, the nephric fold was shown to contain an augmentation factor which is presumed to enhance the activity of this enzyme in vivo. The activity of catalase and glutathione peroxidase, which catalyse the breakdown of H2O2 to O2 and water, were each significantly correlated with the concentration of ferritin.

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Carboxylesterases: General detoxifying enzymes.

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Carboxylesterases: General detoxifying enzymes.

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