Sandbox reserved 916: Difference between revisions
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[[Image:Complete_crystal_structure.png|left|300px|thumb|Crystal Structure of MGL]] | [[Image:Complete_crystal_structure.png|left|300px|thumb|Crystal Structure of MGL]] | ||
==Background== | ==Background== | ||
Monoglyceride lipase is part of the α/β hydrolase family, having a Ser-His-Asp catalytic triad (Celemnte et al. 2012). MGL terminates the signaling of a primary endocannabinoid, 2-AG (Savinainen et al 2010). MGL is able to hydrolyze 2-arachidonoylglycerol into arachidonic acid and glycerol (Bertrand et al. 2010). One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research. | |||
===Metabolic Role=== | ===Metabolic Role=== | ||
===Component of Endocannabinoid System=== | ===Component of Endocannabinoid System=== | ||
Revision as of 12:01, 25 March 2014
Monoglyceride Lipase (MGL)
<StructureSection load= size='450' side='right' scene='58/580299/Human_monoglyceride_lipase/1' caption='Bovine aconitase showing FeS4 cluster complex with sulfate (PDB code 1amj)'>
Background
Monoglyceride lipase is part of the α/β hydrolase family, having a Ser-His-Asp catalytic triad (Celemnte et al. 2012). MGL terminates the signaling of a primary endocannabinoid, 2-AG (Savinainen et al 2010). MGL is able to hydrolyze 2-arachidonoylglycerol into arachidonic acid and glycerol (Bertrand et al. 2010). One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research.
Metabolic Role
Component of Endocannabinoid System
Structure
Catalytic triad
Binding
Ligand Binding Site
Overall Reaction
Literature
Additional Resources
References
