NAAA
Function
Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:22825852, PubMed:30301806). Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine (PubMed:15655246).
Pathway
Lipid metabolism; fatty acid metabolism.
Post-translational modifications
N-glycosylated (PubMed:17980170, PubMed:18793752, PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine.
A disulfide bond is seen in the crystal structure of the human protein, but the Cys residues are not conserved in rodents.
Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:22040171, PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme (PubMed:17980170, PubMed:18793752, PubMed:22040171, PubMed:30301806). The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (Probable) (PubMed:17980170, PubMed:18793752).
Sequence Similarities
Belongs to the acid ceramidase family.
Tissue Specificity
Expressed in numerous tissues, with highest levels in liver and kidney, followed by pancreas.
Cellular localization
- Lysosome
- Membrane
- Peripheral membrane protein
Alternative names
ASAHL, PLT, NAAA, N-acylethanolamine-hydrolyzing acid amidase, Acid ceramidase-like protein, Acylsphingosine deacylase NAAA, N-acylsphingosine amidohydrolase-like, ASAH-like protein