Sandbox Reserved 921: Difference between revisions
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== Function == | == Function == | ||
The fatty acid amide hydrolase cleaves fatty acid amides at the carbon-oxygen double bond in the amide functional group. FAAH uses the active site a catalytic triad consisting of Ser241, Ser217, and Lys142 to degrade the lipids. The hydrogen bonding between the three amino acid residues allows for a partial negative charge at Ser241, 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 used covalently binds to Ser241 disrupting the catalytic triad active site and leaving the hydrolase inactive. Without the enzyme FAAH active, anandamide levels increase causing pain relief due to anandamide interacting with the CB1 and CB2 cannabinoid receptors. | |||
== References == | == References == | ||