1: Amino Acids. 2008 Jan;34(1):127-33. Epub 2007 May 4. A MBP-FAAH fusion protein as a tool to produce human and rat fatty acid amide hydrolase: expression and pharmacological comparison. Labar G, Vliet FV, Wouters J, Lambert DM. Unité de Chimie pharmaceutique et de Radiopharmacie, Ecole de Pharmacie, Faculté de Médecine, Université catholique de Louvain, Bruxelles, Belgium. Fatty acid amide hydrolase (FAAH), a membrane-anchored enzyme responsible for the termination of endocannabinoid signalling, is an attractive target for treating conditions such as pain and anxiety. Inhibitors of the enzyme, optimized using rodent FAAH, are known but their pharmacology and medicinal chemistry properties on the human FAAH are missing. Therefore recombinant human enzyme would represent a powerful tool to evaluate new drug candidates. However, the production of high amounts of enzyme is hampered by the known refractiveness of FAAH to overexpression. Here, we report the successful overexpression of rat and human FAAH as a fusion to the E. coli maltose-binding protein, retaining catalytic properties of native FAAH. Several known FAAH inhibitors were tested and differences in their potencies toward the human and rat FAAH were found, underscoring the importance of using a human FAAH in the development of inhibitors. PMID: 17476568 [PubMed - indexed for MEDLINE] Related Links Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties. [Biochemistry. 1999] PMID:10433686 The fatty acid amide hydrolase (FAAH). [Prostaglandins Leukot Essent Fatty Acids. 2002] PMID:12052036 Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana. [J Biol Chem. 2003] PMID:12824167 The fatty acid amide hydrolase (FAAH). [Chem Phys Lipids. 2000] PMID:11106785 Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. [Biochemistry. 1998] PMID:9790682