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ABHD4 hydrolyses NAPE
Stable Identifier
R-HSA-5694583
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
,
endoplasmic reticulum membrane
ReviewStatus
5/5
Locations in the PathwayBrowser
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Metabolism (Homo sapiens)
Metabolism of lipids (Homo sapiens)
Phospholipid metabolism (Homo sapiens)
Glycerophospholipid biosynthesis (Homo sapiens)
Acyl chain remodelling of PE (Homo sapiens)
ABHD4 hydrolyses NAPE (Homo sapiens)
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The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Abhydrolase domain-containing protein 4 (ABHD4) is a regulator of endocannabinoid signalling and suppressor of tumor growth. Its physiological substrates are both N-acyl phosphatidylethanolamine (NAPE) and a wide range of lysoNAPEs. Shown here, ANHD4 mediates the hydrolysis of NAPE to glycerophospho-arachidonyl ethanolamine (GPAEA), an endocannabanoid (Simon & Cravatt 2006).
Literature References
PubMed ID
Title
Journal
Year
16818490
Endocannabinoid biosynthesis proceeding through glycerophospho-N-acyl ethanolamine and a role for alpha/beta-hydrolase 4 in this pathway
Simon, GM
,
Cravatt, BF
J. Biol. Chem.
2006
Participants
Input
H2O [cytosol]
NAPE [endoplasmic reticulum membrane]
Output
acyl group [endoplasmic reticulum membrane]
GPAEA [endoplasmic reticulum membrane]
Participates
as an event of
Acyl chain remodelling of PE (Homo sapiens)
Catalyst Activity
hydrolase activity of ABHD4 [endoplasmic reticulum membrane]
Physical Entity
ABHD4 [endoplasmic reticulum membrane]
(Homo sapiens)
Activity
hydrolase activity (GO:0016787)
Orthologous Events
ABHD4 hydrolyses NAPE (Bos taurus)
ABHD4 hydrolyses NAPE (Caenorhabditis elegans)
ABHD4 hydrolyses NAPE (Canis familiaris)
ABHD4 hydrolyses NAPE (Drosophila melanogaster)
ABHD4 hydrolyses NAPE (Mus musculus)
ABHD4 hydrolyses NAPE (Rattus norvegicus)
ABHD4 hydrolyses NAPE (Saccharomyces cerevisiae)
ABHD4 hydrolyses NAPE (Schizosaccharomyces pombe)
ABHD4 hydrolyses NAPE (Sus scrofa)
ABHD4 hydrolyses NAPE (Xenopus tropicalis)
Authored
Jassal, B (2015-05-22)
Reviewed
D'Eustachio, P (2015-06-26)
Created
Jassal, B (2015-05-22)
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