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

Stable Identifier
Reaction [transition]
Homo sapiens
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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
15272052 RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol

Kathuria, S, Dinh, TP, Piomelli, D

Mol Pharmacol 2004
19962385 Structural basis for human monoglyceride lipase inhibition

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

J Mol Biol 2010
18452279 Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification

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

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

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

Chembiochem 2010
Catalyst Activity

acylglycerol lipase activity of MGLL dimer [endoplasmic reticulum membrane]

Orthologous Events
Cross References
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