Evidence for Distinct Roles in Catalysis for Residues of the Serine-Serine-Lysine Catalytic Triad of Fatty Acid Amide Hydrolase

• Published in: The Journal of biological chemistry Vol. 278; no. 39; pp. 37393 - 37399
• Main Authors: McKinney, Michele K., Cravatt, Benjamin F.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.09.2003; American Society for Biochemistry and Molecular Biology
• Subjects: Amidohydrolases - chemistry; Amidohydrolases - metabolism; Animals; Catalysis; Hydrolysis; Kinetics; Lysine; Mutation; Rats; Serine; Structure-Activity Relationship

Fatty acid amide hydrolase (FAAH) is a mammalian amidase signature enzyme that inactivates neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing substance oleamide. The recent determination of the three-dimensional structures of FAAH and two distan...