The enzyme fatty acyl amide hydrolase (FAAH) is widely expressed in brain and other tissues, and is capable of hydrolyzing anandamide (AEA) and other simple esters and amides with long unsaturated acyl chains.1 JP83 is an irreversible FAAH inhibitor of the carbamate class with an IC50 of 14 nM for the human recombinant enzyme when tested using radiolabeled oleamide as the substrate.2
1
Zhang, Y.H., Zhang, G.Y., Mollat, P., et al. Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein. J Biol Chem26818875-18881(1993).
2
Alexander, J.P., and Cravatt, B.F. Mechanism of carbmate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem Biol121179-1187(2005).
Zhang, Y.H., Zhang, G.Y., Mollat, P., et al. Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein. J Biol Chem26818875-18881(1993).
Alexander, J.P., and Cravatt, B.F. Mechanism of carbmate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem Biol121179-1187(2005).
JP83 is available in the following screening
library: