1. Ex vivo lipidomics reveal monoacylglycerols as substrates for a fatty acid amide hydrolase in the legume Medicago truncatula.
- Author
-
Arias-Gaguancela O, Herrell E, and Chapman KD
- Subjects
- Substrate Specificity, Plant Proteins metabolism, Plant Proteins genetics, Plant Proteins chemistry, Ethanolamines metabolism, Ethanolamines chemistry, Gas Chromatography-Mass Spectrometry, Hydrolysis, Medicago truncatula enzymology, Medicago truncatula metabolism, Medicago truncatula genetics, Amidohydrolases metabolism, Amidohydrolases chemistry, Amidohydrolases genetics, Lipidomics methods, Monoglycerides metabolism, Monoglycerides chemistry
- Abstract
Fatty acid amide hydrolase (FAAH) is a conserved hydrolase in eukaryotes with promiscuous activity toward a range of acylamide substrates. The native substrate repertoire for FAAH has just begun to be explored in plant systems outside the model Arabidopsis thaliana. Here, we used ex vivo lipidomics to identify potential endogenous substrates for Medicago truncatula FAAH1 (MtFAAH1). We incubated recombinant MtFAAH1 with lipid mixtures extracted from M. truncatula and resolved their profiles via gas chromatography-mass spectrometry (GC-MS). Data revealed that besides N-acylethanolamines (NAEs), sn-1 or sn-2 isomers of monoacylglycerols (MAGs) were substrates for MtFAAH1. Combined with in vitro and computational approaches, our data support both amidase and esterase activities for MtFAAH1. MAG-mediated hydrolysis via MtFAAH1 may be linked to biological roles that are yet to be discovered., (© 2024 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
- Published
- 2024
- Full Text
- View/download PDF