EC 3.5.1.60 - N-(long-chain-acyl)ethanolamine deacylase

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IntEnz Enzyme Nomenclature
EC 3.5.1.60

Names

Accepted name:
N-(long-chain-acyl)ethanolamine deacylase
Other names:
N-acylethanolamine amidohydrolase
acylethanolamine amidase
Systematic name:
N-(long-chain-acyl)ethanolamine amidohydrolase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047412
CAS Registry Number: 99283-61-1
UniProtKB/Swiss-Prot:

References

  1. Ueda, N., Yamanaka, K., Yamamoto, S.
    Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance.
    J. Biol. Chem. 276 : 35552-35557 (2001). [PMID: 11463796]
  2. Ueda, N., Yamanaka, K., Terasawa, Y., Yamamoto, S.
    An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors.
    FEBS Lett. 454 : 267-270 (1999). [PMID: 10431820]
  3. West, J. M., Zvonok, N., Whitten, K. M., Wood, J. T., Makriyannis, A.
    Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase.
    J. Proteome Res. 11 : 972-981 (2012). [PMID: 22040171]
  4. Zhao, L. Y., Tsuboi, K., Okamoto, Y., Nagahata, S., Ueda, N.
    Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
    Biochim. Biophys. Acta 1771 : 1397-1405 (2007). [PMID: 17980170]

[EC 3.5.1.60 created 1989]