Cited by 185Cannabis and Cannabinoid ResearchSphingolipid Metabolism and SignalingLipid metabolism and biosynthesis

The N‐Acylethanolamine‐Hydrolyzing Acid Amidase (NAAA)

Tsuboi, Kazuhito, Takezaki, Naoko, Ueda, Natsuo·2007·Chemistry & Biodiversity

Abstract

Bioactive N‐acylethanolamines, including the endocannabinoid anandamide and anti‐inflammatory N‐palmitoylethanolamine, are hydrolyzed to fatty acids and ethanolamine in animal tissues by the catalysis of fatty acid amide hydrolase (FAAH). We recently cloned cDNA of N‐acylethanolamine‐hydrolyzing acid amidase (NAAA), another enzyme catalyzing the same reaction, from human, rat, and mouse. NAAA reveals no sequence homology with FAAH and belongs to the choloylglycine hydrolase family. The most striking catalytic property of NAAA is pH optimum at 4.5–5, which is consistent with its immunocytochemical localization in lysosomes. In rat, NAAA is highly expressed in lung, spleen, thymus, and intestine. Notably, the expression level of NAAA is exceptionally high in rat alveolar macrophages. The primary structure of NAAA exhibits 33–35% amino acid identity to that of acid ceramidase, a lysosomal enzyme hydrolyzing ceramide to fatty acid and sphingosine. NAAA actually showed a low, but detectable ceramide‐hydrolyzing activity, while acid ceramidase hydrolyzed N‐lauroylethanolamine. Thus, NAAA is a novel lysosomal hydrolase, which is structurally and functionally similar to acid ceramidase. These results suggest a unique role of NAAA in the degradation of N‐acylethanolamines.

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Crossref · 10.1002/cbdv.200790159

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Authors
Tsuboi, K., Takezaki, N., & Ueda, N.
Affiliations
Kagawa University (JP)
Venue
Chemistry & Biodiversity
Publisher
Wiley
Published
2007-08
Volume
4
Issue
8
Pages
1914-1925
ISSN
  • 1612-1872 (ISSN-L)
  • 1612-1880
OpenAlex
W2045872436
Cited by
172
References
73
Citations by year
2026: 1 · 2025: 5 · 2024: 7 · 2023: 5 · 2022: 7 · 2021: 13 · 2020: 10 · 2019: 11 · 2018: 11 · 2017: 8 · 2016: 11 · 2015: 8 · 2014: 13 · 2013: 10 · 2012: 15
FWCI
1.19
Type
journal article
Language
en
Open access
closed
Locations
  • Chemistry & Biodiversity (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Pharmacology › Cannabis and Cannabinoid Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords
NAAA, fatty acid amide hydrolase, N-acylethanolamines, anandamide, N-palmitoylethanolamine, lysosomal enzymes, acid ceramidase, ceramide hydrolysis, tissue expression, alveolar macrophages, pH optimum, endocannabinoid degradation
MeSH terms
Amidohydrolases, Amino Acid Sequence, Animals, Galactosylgalactosylglucosylceramidase, Ethanolamines, Humans, Hydrolysis, Molecular Sequence Data

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