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Updated: Dec 31, 2025

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Fatty Acid Amide Hydrolases: An Expanded Capacity for Chemical Communication?
1BioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA.
Abstract:
Fatty acid amide hydrolase (FAAH) is an enzyme that belongs to the amidase signature (AS) superfamily and is widely distributed in multicellular eukaryotes. FAAH hydrolyzes lipid signaling molecules - namely, N-acylethanolamines (NAEs) - which terminates their actions. Recently, the crystal structure of Arabidopsis thaliana FAAH was solved and key residues were identified for substrate-specific interactions. Here, focusing on residues surrounding the substrate-binding pocket, a comprehensive analysis of FAAH sequences from angiosperms reveals a distinctly different family of FAAH-like enzymes. We hypothesize that FAAH, in addition to its role in seedling development, also acts in an N-acyl amide communication axis to facilitate plant-microbe interactions and that structural diversity provides for the flexible use of a wide range of small lipophilic signaling molecules.
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