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Fatty acid amide hydrolase (FAAH) dimer shown with covalent inhibitor (MAFP, yellow) bound in the active site.
Fatty acid amide hydrolase
Symbol FAAH
Entrez 2166
HUGO 3553
OMIM 602935
RefSeq NM_001441
UniProt O00519
Other data
EC number 3.5.1.-
Locus Chr. 1 p35-p34

Fatty acid amide hydrolase or FAAH is an integral membrane protein (IMP) that hydrolyzes bioactive amides including the endocannabinoid anandamide (an agonist of cannabinoid receptors and TRPV1 vanilloid receptors) and agonists of the peroxisome proliferator-activated receptors such as N-oleoylethanolamine and N-palmitoylethanolamine to free fatty acid and ethanolamine.[1] It is also the primary terminator of the hypnotic lipid oleamide as well as the less well-characterized N-acyl taurines.

Due to its ability to regulate anandamide levels, it is currently viewed as an attractive drug target. A human mutation (proline 129 to threonine) has been associated with problem drug use.[2] Additionally, genetic ablation or pharmacological inhibition of FAAH results in analgesia (lack of sensitivity to pain) in mice due, perhaps, to the effects of anandamide on cannabinoid receptors.

FAAH was cloned in 1996 by Ben Cravatt at The Scripps Research Institute where it continues to be intensively studied and characterized.[3][4]

Inhibitors and assays

Both non-selective and selective inhibitors of the enzyme have been described. Examples of non-selective inhibitors include PMSF (phenylmethylsulfonylfluoride), MAFP, and ATMK (arachidonoyltrifluoromethylketone), while URB597 is widely regarded as the current 'gold standard' FAAH inhibitor.[citation needed] The enzyme is typically assayed making use of a radiolabelled anandamide substrate, which generates free labelled ethanolamine, although alternative spectrophotometric methods have also been described.


  1. ^ McKinney M.K., Cravatt B.F., "Structure and Function of Fatty Acid Amide Hydrolase." Ann. Rev. Biochem. 74:411(2005). PMID 15952893
  2. ^ Sipe J.C., Chiang K., Gerber A.L., Beutler E., Cravatt B.F., "A missense mutation in human fatty acid amide hydrolase associated with problem drug use." Proc. Natl. Acad. Sci. U.S.A. 99:8394-8399(2002). PMID 12060782
  3. ^ Cravatt B.F., Giang D.K., Mayfield S.P., Boger D.L., Lerner, R.A.; "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides"; Nature 384:83 (1996). PMID 8900284
  4. ^ Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling". Science 298 (5599): 1793-6. doi:10.1126/science.1076535. PMID 12459591.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "FAAH". A list of authors is available in Wikipedia.
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