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  1. ; ; (, FEBS Letters)
    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 modelArabidopsis thaliana. Here, we usedex vivolipidomics to identify potential endogenous substrates forMedicago truncatulaFAAH1 (MtFAAH1). We incubated recombinant MtFAAH1 with lipid mixtures extracted fromM. truncatulaand resolved their profiles via gas chromatography–mass spectrometry (GC–MS). Data revealed that besidesN‐acylethanolamines (NAEs),sn‐1orsn‐2isomers of monoacylglycerols (MAGs) were substrates for MtFAAH1. Combined within vitroand 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. 
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