Fatty Acid Amide Hydrolases: An Expanded Capacity for Chemical Communication?

Mina Aziz; Kent D Chapman

doi:10.1016/j.tplants.2019.11.002

Fatty Acid Amide Hydrolases: An Expanded Capacity for Chemical Communication?

Trends Plant Sci. 2020 Mar;25(3):236-249. doi: 10.1016/j.tplants.2019.11.002. Epub 2020 Jan 7.

Authors

Mina Aziz¹, Kent D Chapman²

Affiliations

¹ BioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA. Electronic address: Mina.Aziz@unt.edu.
² BioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA. Electronic address: Kent.Chapman@unt.edu.

PMID: 31919033
DOI: 10.1016/j.tplants.2019.11.002

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.

Keywords: N-acyl l-homoserine lactones; N-acylethanolamines; alkamides; fatty acid amide hydrolase; plant–microbe interactions; quorum sensing.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review

MeSH terms

Amidohydrolases*
Arabidopsis*

Substances

Amidohydrolases
fatty-acid amide hydrolase