FAAH
Fatty acid amide hydrolase (FAAH), belonging to an amidase-signature (AS) protein family, is a membrane-bound protein predominantly in microsomal and mitochondrial fractions that catalyzes the hydrolysis of several bioactive lipids, including anandamide, 2-arachidonoylglycerol (2-AG) and oleamide. The mammalian FAAHs are 63 kDa (579 amino acids in length) proteins characterized by containing several domains defined by homology and function, including, a highly conserved seine-and-glycine-rich AS domain, a predicted transmembrane domain and a proline rich domain. Results of mutation studies suggest, unlike other members of AS protein family, the catalytic activity of FAAH is not associated with the Ser-His-Asp triad but possibly with Ser217 and Lys142.
- C5719 Oleyl Trifluoromethyl KetoneSummary: potent inhibitor of FAAH
- B5562 TC-F 2Summary: FAAH inhibitor
- B5704 SA 57Summary: FAAH inhibitor
- B5714 SA 47Summary: FAAH inhibitor
- B4931 TAK 21dSummary: Potent FAAH inhibitor
- C4122 JNJ-42165279Summary: FAAH inhibitor
- C4251 Oleoyl Ethyl AmideSummary: FAAH inhibitor with potential analgesic and anxiolytic activity
- C4279 4-(n-nonyl) Benzeneboronic AcidSummary: FAAH and MAGL inhibitor
- C4756 PF-622Summary: potent, time-dependent, irreversible FAAH inhibitor
- C4983 JP83Summary: irreversible fatty acyl amide hydrolase (FAAH) inhibitor