BioPAX pathway converted from "FAAH hydrolyses AEA to AA and ETA" in the Reactome database. FAAH hydrolyses AEA to AA and ETA FAAH hydrolyses AEA to AA and ETA Fatty acid amides are a class of lipid transmitters that include the endogenous cannabinoid anandamide (AEA) and the sleep-inducing chemical oleamide. The magnitude and duration of their signalling are controlled by enzymatic hydrolysis mediated by fatty-acid amide hydrolases 1 and 2 (FAAH, H2). Hydrolysis of AEA is described here (Wei et al. 2006). FAAH is localised to the ER membrane whereas FAAH2 is localised to lipid droplets (Kaczocha et al. 2010). Authored: Jassal, Bijay, 2015-05-18 Reviewed: D'Eustachio, Peter, 2015-06-26 Edited: Jassal, Bijay, 2015-05-18 Reactome DB_ID: 5693754 1 cytosol GO 0005829 anandamide [ChEBI:2700] anandamide Reactome ChEBI 2700 Reactome DB_ID: 29356 1 water [ChEBI:15377] water ChEBI 15377 Reactome DB_ID: 29768 1 arachidonate [ChEBI:32395] arachidonate (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate (20:4n6) (5Z,8Z,11Z,14Z)-eicosatetraenoate ChEBI 32395 Reactome DB_ID: 1498751 1 ethanolamine [ChEBI:16000] ethanolamine ChEBI 16000 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Reactome DB_ID: 5693746 endoplasmic reticulum membrane GO 0005789 UniProt:O00519 FAAH FAAH FAAH FAAH1 FUNCTION Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:9122178, PubMed:17015445, PubMed:19926788). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed:9122178, PubMed:17015445). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:21049984). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).ACTIVITY REGULATION Inhibited by O-aryl carbamates and alpha-keto heterocycles (PubMed:17015445). Inhibited by trifluoromethyl ketone (PubMed:9122178).SUBUNIT Homodimer.TISSUE SPECIFICITY Highly expressed in the brain, small intestine, pancreas, skeletal muscle and testis. Also expressed in the kidney, liver, lung, placenta and prostate.POLYMORPHISM Genetic variations in FAAH can be associated with susceptibility to polysubstance abuse [MIM:606581]. At homozygosity, variant Thr-129 is strongly associated with drug and alcohol abuse, and methamphetamine dependence.SIMILARITY Belongs to the amidase family. Homo sapiens NCBI Taxonomy 9606 UniProt O00519 Chain Coordinates 1 EQUAL 579 EQUAL GO 0017064 GO molecular function Reactome Database ID Release 82 5693749 Database identifier. Use this URL to connect to the web page of this instance in Reactome: Reactome Database ID Release 82 5693742 Database identifier. Use this URL to connect to the web page of this instance in Reactome: Reactome R-HSA-5693742 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: 19926788 Pubmed 2010 Lipid droplets are novel sites of N-acylethanolamine inactivation by fatty acid amide hydrolase-2 Kaczocha, Martin Glaser, Sherrye T Chae, Janiper Brown, Deborah A Deutsch, Dale G J. Biol. Chem. 285:2796-806 17015445 Pubmed 2006 A second fatty acid amide hydrolase with variable distribution among placental mammals Wei, Binqing Q Mikkelsen, Tarjei S McKinney, Michele K Lander, Eric S Cravatt, BF J. Biol. Chem. 281:36569-78