Identification of an arylalkylamine N-acyltransferase from Drosophila melanogaster that catalyzes the formation of long-chain N-acylserotonins

•Recombinant D. melanogaster AANATL2 was expressed and purified from E. coli.•AANATL2 was found to catalyze the formation of long-chain N-acylarylalkylamides.•AANATL2 transcripts were localized to the D. melanogaster thorax-abdomen by RT-PCR.•Endogenous levels of long-chain N-acylserotonins were quantified from the fly.•AANATL2 and long-chain N-acylserotonins were co-localized to the thorax-abdomen. Arylalkylamine N-acyltransferase-like 22The authors recommend the change of arylalkylamine N-acetyltransferase to arylalkylamine N-acyltransferase due to the discovery of acyl-CoA substrates longer than C2 (acetyl).2 (AANATL2) from Drosophila melanogaster was expressed and shown to catalyze the formation of long-chain N-acylserotonins and N-acydopamines. Subsequent identification of endogenous amounts of N-acylserotonins and colocalization of these fatty acid amides and AANATL2 transcripts gives supporting evidence that AANATL2 has a role in the biosynthetic formation of these important cell signalling lipids.