2-MAG is hydrolyzed to fatty acid and glycerol by MGLL

Stable Identifier
R-HSA-1482543
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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At the endoplasmic reticulum (ER) membrane, monoglyceride lipase (MGLL) hydrolyzes 2-monoacylglycerol (2-MAG) to form a fatty acid and glycerol (Dinh et al. 2004, Zvonok et al. 2008, Bertrand et al. 2010, Labar et al. 2010).

Literature References
PubMed ID Title Journal Year
19962385 Structural basis for human monoglyceride lipase inhibition

Bertrand, T, Augé, F, Houtmann, J, Rak, A, Vallée, F, Mikol, V, Berne, PF, Michot, N, Cheuret, D, Hoornaert, C, Mathieu, M

J Mol Biol 2010
15272052 RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol

Dinh, TP, Kathuria, S, Piomelli, D

Mol Pharmacol 2004
18452279 Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification

Zvonok, N, Williams, J, Johnston, M, Pandarinathan, L, Janero, DR, Li, J, Krishnan, SC, Makriyannis, A

J Proteome Res 2008
19957260 Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling

Labar, G, Bauvois, C, Borel, F, Ferrer, JL, Wouters, J, Lambert, DM

Chembiochem 2010
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Catalyst Activity
Title
acylglycerol lipase activity of MGLL dimer [endoplasmic reticulum membrane]
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