Fatty-acid amide hydrolase
AssigneeThe Scripps Research Institute
InventorsNorton B. Gilula, Benjamin F. Cravatt, Richrd A. Lerner
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Abstract
The soporific activity of cis-9,10-octadecenoamide and other soporific fatty acid primary amides is neutralized by hydrolysis in the presence of fatty-acid amide hydrolase (FAAH). Hydrolysis of cis-9,10-octadecenoamide by FAAH leads to the formation of oleic acid, a compound without soporific activity. FAAH has be isolated and the gene encoding FAAH has been cloned, sequenced, and used to express recombinant FAAH. Inhibitors of FAAH are disclosed to block the hydrolase activity.
Claims3
An isolated or purified fatty-acid amide hydrolase (FAAH) encoded by the nucleotide sequence shown in SEQ ID No. 42.
An isolated or purified fatty-acid amide hydrolase (FAAH) encoded by the nucleotide sequence shown in SEQ ID No. 39.
An isolated or purified fatty-acid amide hydrolase (FAAH) encoded by the nucleotide sequence shown in SEQ ID No. 35.
Dependencies are inferred from the claim text.