biostudies-literatureUnknown3(5)Armirotti AThe cysteine amidase N-acylethanolamine acid amidase (NAAA) is a member of the N-terminal nucleophile class of enzymes and a potential target for anti-inflammatory drugs. We investigated the mechanism of inhibition of human NAAA by substituted β-lactones. We characterized pharmacologically a representative member of this class, ARN077, and showed, using high-resolution liquid chromatography-tandem mass spectrometry, that this compound forms a thioester bond with the N-terminal catalytic cysteine in human NAAA.ACS medicinal chemistry letters422-6https://www.ebi.ac.uk/biostudies/studies/S-EPMC4025845biostudies-literatureβ-Lactones Inhibit N-acylethanolamine Acid Amidase by S-Acylation of the Catalytic N-Terminal Cysteine.PMC4025845Karacsonyi CBertozzi FTarzia GPonzano SRomeo EDionisi MGarau GTarozzo GBandiera TMor MArmirotti AMengatto LPiomelli DReggiani Afalseβ-Lactones Inhibit N-acylethanolamine Acid Amidase by S-Acylation of the Catalytic N-Terminal Cysteine.The cysteine amidase N-acylethanolamine acid amidase (NAAA) is a member of the N-terminal nucleophile class of enzymes and a potential target for anti-inflammatory drugs. We investigated the mechanism of inhibition of human NAAA by substituted β-lactones. We characterized pharmacologically a representative member of this class, ARN077, and showed, using high-resolution liquid chromatography-tandem mass spectrometry, that this compound forms a thioester bond with the N-terminal catalytic cysteine in human NAAA.2012-01-01T00:00:00Z2012 May2025-04-04T08:41:59.8Z2019-03-27T01:28:29ZS-EPMC40258452490048710.1021/ml300056y