Document Detail


The N-acylethanolamine-hydrolyzing acid amidase (NAAA).
MedLine Citation:
PMID:  17712833     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Kazuhito Tsuboi; Naoko Takezaki; Natsuo Ueda
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Chemistry & biodiversity     Volume:  4     ISSN:  1612-1880     ISO Abbreviation:  Chem. Biodivers.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-08-27     Completed Date:  2007-09-28     Revised Date:  2012-03-27    
Medline Journal Info:
Nlm Unique ID:  101197449     Medline TA:  Chem Biodivers     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  1914-25     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Kagawa University School of Medicine, 1750-1 Ikenobe, Miki, Kagawa 761-0793, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amidohydrolases / chemistry,  genetics*,  metabolism*
Amino Acid Sequence
Animals
Ethanolamines / chemistry,  metabolism*
Galactosylgalactosylglucosylceramidase / genetics,  metabolism
Humans
Hydrolysis
Molecular Sequence Data
Chemical
Reg. No./Substance:
0/Ethanolamines; 0/N-acylethanolamines; EC 3.2.1.47/Galactosylgalactosylglucosylceramidase; EC 3.5.-/Amidohydrolases; EC 3.5.1.-/NAAA protein, human; EC 3.5.1.4/amidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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