2-AG hydrolysis to arachidonate by MAGL

Stable Identifier
R-HSA-426043
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
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2-AG hydrolysis to arachidonate by MAGL
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Monoacylglycerol lipase (MAGL) is a key enzyme in the hydrolysis of the endocannabinoid 2-arachidonoylglycerol to arachidonate and glycerol. In adipocytes MAGL and hormone-sensitive lipase (LIPE) hydrolyze intracellular triglyceride stores. MAGL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
Literature References
Participants
Input
Output
Participates
as an event of
Catalyst Activity

monoacylglycerol lipase activity of MGLL [plasma membrane]

Physical Entity
MGLL [plasma membrane] (Homo sapiens)
Activity
monoacylglycerol lipase activity (GO:0047372)
Orthologous Events
2-AG hydrolysis to arachidonate by MAGL (Bos taurus)
2-AG hydrolysis to arachidonate by MAGL (Canis familiaris)
2-AG hydrolysis to arachidonate by MAGL (Danio rerio)
2-AG hydrolysis to arachidonate by MAGL (Dictyostelium discoideum)
2-AG hydrolysis to arachidonate by MAGL (Gallus gallus)
2-AG hydrolysis to arachidonate by MAGL (Mus musculus)
2-AG hydrolysis to arachidonate by MAGL (Rattus norvegicus)
2-AG hydrolysis to arachidonate by MAGL (Saccharomyces cerevisiae)
2-AG hydrolysis to arachidonate by MAGL (Schizosaccharomyces pombe)
2-AG hydrolysis to arachidonate by MAGL (Sus scrofa)
2-AG hydrolysis to arachidonate by MAGL (Xenopus tropicalis)
Cross References
RHEA
Authored
Jupe, S  (2009-06-11)
Reviewed
Akkerman, JW  (2009-09-04)
Created
Jupe, S  (2009-06-11)
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