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Fatty Acid Amide Hydrolase

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Encyclopedia of Signaling Molecules
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Synonyms

Anandamide amidohydrolase; Oleamide hydrolase

Historical Background

A membrane-associated enzyme activity from rat liver that hydrolyzes N-acylethanolamine (NAE) species containing unsaturated and monounsaturated acyl chains was first described in 1985 by Schmid and colleagues (1985). Subsequently, an enzyme activity with similar properties that breaks the sleep-inducing substance cis-9-octadecenamide (oleamide) was reported and suggested to represent a general mechanism for terminating NAEs signaling in vivo. Nonetheless, the actual enzymes involved in NAEs metabolism remained unknown until the late 1990s, when Cravatt and colleagues purified this amidohydrolase activity from rat liver membranes (Cravatt et al. 1996). This enzyme, named fatty acid amide hydrolase (FAAH; E.C. 3.5.1.4), was shown to be specifically inhibitable (Deutsch et al. 1997), was recombinantly expressed, and was found to hydrolyze several endogenous NAEs, including the neuromodulator/neurotransmitter N-a...

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Acknowledgments

We are grateful to Prof. Enrico Dainese (University of Teramo, Teramo, Italy) for kindly providing FAAH three-dimensional structure. This study was partially supported by the Italian Ministero dell’Istruzione, dell’Università e della Ricerca (PRIN 2012 to F.F. and PRIN 2010–2011 to M.M.).

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Correspondence to Mauro Maccarrone .

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Fezza, F., Bari, M., Fazio, D., Maccarrone, M. (2018). Fatty Acid Amide Hydrolase. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101566

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