Structural highlights
Function
[FAAH1_RAT] Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (By similarity).
Publication Abstract from PubMed
In addition to inhibiting the cyclooxygenase (COX)-mediated biosynthesis of prostanoids, various widely used nonsteroidal anti-inflammatory drugs (NSAIDs) enhance endocannabinoid signaling by blocking the anandamide-degrading membrane enzyme fatty acid amide hydrolase (FAAH). The X-ray structure of FAAH in complex with the NSAID carprofen, along with site-directed mutagenesis, enzyme activity assays, and NMR analysis, has revealed the molecular details of this interaction, providing information that may guide the design of dual FAAH-COX inhibitors with superior analgesic efficacy.
A Binding Site for Nonsteroidal Anti-inflammatory Drugs in Fatty Acid Amide Hydrolase.,Bertolacci L, Romeo E, Veronesi M, Magotti P, Albani C, Dionisi M, Lambruschini C, Scarpelli R, Cavalli A, De Vivo M, Piomelli D, Garau G J Am Chem Soc. 2013 Jan 9;135(1):22-5. doi: 10.1021/ja308733u. Epub 2012 Dec 21. PMID:23240907[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bertolacci L, Romeo E, Veronesi M, Magotti P, Albani C, Dionisi M, Lambruschini C, Scarpelli R, Cavalli A, De Vivo M, Piomelli D, Garau G. A Binding Site for Nonsteroidal Anti-inflammatory Drugs in Fatty Acid Amide Hydrolase. J Am Chem Soc. 2013 Jan 9;135(1):22-5. doi: 10.1021/ja308733u. Epub 2012 Dec 21. PMID:23240907 doi:http://dx.doi.org/10.1021/ja308733u
