Fatty-acid amide hydrolase
AssigneeThe Scripps Research Institute
InventorsNorton B. Gilula, Benjamin F. Cravatt, Richard A. Lerner
Life of this patent
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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.
Claims6
An isolated and purified polypeptide that has the amino acid residue sequence shown in SEQ ID NO 36.
An isolated and purified polypeptide that has the amino acid residue sequence shown in SEQ ID NO 40.
An isolated and purified polypeptide that has the amino acid residue sequence shown in SEQ ID NO 43.
Dependencies are inferred from the claim text.