NAAA hydrolyses NAEs to FAs and ethanolamine

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Catalyst Activity

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

Orthologous Events
Cite Us!