| 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, Gene, KEGG, MetaCyc, PDB, 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] |
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| [EC 3.5.1.60 created 1989, modified 2019] |
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