The Enzyme Database

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EC 3.5.1.60     
Accepted name: N-(long-chain-acyl)ethanolamine deacylase
Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other name(s): NAAA (gene name); N-acylethanolamine amidohydrolase; acylethanolamine amidase
Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase
Comments: This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC 3.5.1.99, fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99283-61-1
References:
1.  Ueda, N., Yamanaka, K. and Yamamoto, S. Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance. J. Biol. Chem 276 (2001) 35552–35557. [PMID: 11463796]
2.  Ueda, N., Yamanaka, K., Terasawa, Y. and Yamamoto, S. An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors. FEBS Lett. 454 (1999) 267–270. [PMID: 10431820]
3.  West, J.M., Zvonok, N., Whitten, K.M., Wood, J.T. and Makriyannis, A. Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J Proteome Res 11 (2012) 972–981. [PMID: 22040171]
4.  Zhao, L.Y., Tsuboi, K., Okamoto, Y., Nagahata, S. and Ueda, N. Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism. Biochim. Biophys. Acta 1771 (2007) 1397–1405. [PMID: 17980170]
[EC 3.5.1.60 created 1989, modified 2019]
 
 


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