Sandbox Reserved 921: Difference between revisions

The fatty acid amide hydrolase <scene name='57/573135/4j5p_dimer/3'>dimer</scene> is an integral membrane protein that cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group.  The lipid-degrading activity of FAAH derives from its unusual <scene name='57/573135/Catalytic_triad/2'>catalytic triad</scene>, consisting of Ser241, Ser217, and Lys142.  The hydrogen bonding between the three amino acid residues allows for a partial negative charge at <scene name='57/573135/Ser241_4j5p/1'>Ser241</scene>, which acts as a nucleophile in the enzymatic reaction.  The Ser241 residue binds with the carbon in the amide group, cleaves the fatty acid amide, and is protonated by water.  The inhibitor BR1 covalently binds to Ser241 disrupting the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] active site and inactivating the [http://en.wikipedia.org/wiki/Hydrolase hydrolase].<ref name= "4HBP">PMID:23218778</ref>  Without the active FAAH, anandamide accumulates, resulting in pain relief due to its increased concentration and interaction with the CB1 and CB2 cannabinoid receptors.