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- Andrea Armirotti, Elisa Romeo, Stefano Ponzano, Luisa Mengatto, Mauro Dionisi, Claudia Karacsonyi, Fabio Bertozzi, Gianpiero Garau, Glauco Tarozzo, Angelo Reggiani, Tiziano Bandiera, Giorgio Tarzia, Marco Mor, and Daniele Piomelli.
- Department of Drug Discovery and Development, Istituto Italiano di Tecnologia , via Morego, 30, 16163 Genova, Italy.
- Acs Med Chem Lett. 2012 May 10;3(5):422-6.
AbstractThe 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.
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