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.
顺式-9,10-
十八碳烯酰胺和其他催眠
脂肪酸原生胺的催眠活性在
脂肪酸酰胺
水解酶(FAAH)的存在下被中和。FAAH对顺式-9,10-
十八碳烯酰胺的
水解导致
油酸的形成,这是一种没有催眠活性的化合物。FAAH已被分离,FAAH编码
基因已被克隆,测序并用于表达
重组FAAH。抑制FAAH的
抑制剂被披露可阻断
水解酶活性。