NAAA hydrolyses NAEs to FAs and ethanolamine

Stable Identifier
R-HSA-6803753
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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N-acylethanolamines (NAEs) are bioactive lipid molecules present in animals and plants. N-acylethanolamine-hydrolyzing acid amidase (NAAA), a heterodimeric lysosomal enzyme is able to hydrolyse NAEs to their respective fatty acids (FAs) and ethanolamine (ETA). The NAEs N-arachidonoylethanolamine (anandamide), N-palmitoylethanolamine, and N-oleoylethanolamine possess cannabimimetic activity, anti-inflammatory and analgesic activities, and anorexic activity, respectively. NAAA can mediate their endogenous levels and shows greatest affinity for N-palmitoylethanolamine (Hong et al. 1999, Tsuboi et al. 2005).
Literature References
PubMed ID Title Journal Year
10610717 Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein

Park, JH, Schuchman, EH, He, X, Levy, B, Li, CM, Hong, SB, Yoo, OJ, Rhee, HJ

Genomics 1999
15655246 Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase

Sun, YX, Okamoto, Y, Tonai, T, Ueda, N, Tsuboi, K, Araki, N

J. Biol. Chem. 2005
Participants
Participates
Catalyst Activity

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds of NAAA dimer [lysosomal lumen]

Orthologous Events
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