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Dominique Stephens, Erica Yothment

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 [[Image:Complete_crystal_structure.png|left|300px|thumb|'''Figure 1:'''Crystal Structure of MGL Alpha helixes are in blue and beta sheets in purple. This protein is a dimer that is linked by antiparallel beta sheets]]
 ==Background==
-Monoglyceride [[:Category:Lipase| Lipase]] (MGL) is part of the α/β hydrolase family,a [[:Category:Serine hydrolase| Serine hydrolase]] (Figure 1), having a <scene name='58/580298/Catalytic_triad/4'>Ser-His-Asp catalytic triad </scene> <ref name="Clemente">[Clemente, J. C., E. Nulton, M. Nelen, M. J. Todd, D. Maguire, C. Schalk-Hihi, L. C. Kuo, S.-P. Zhang, C. M. Flores, and J. K. Kranz. "Screening and Characterization of Human Monoglyceride Lipase Active Site Inhibitors Using Orthogonal Binding and Functional Assays." Journal of Biomolecular Screening 17.5 (2012): 629-40]</ref>. [http://en.wikipedia.org/wiki/Monoacylglycerol_lipase MGL] is present in most cells, providing the rate limiting step for  the hydrolysis of [http://en.wikipedia.org/wiki/Monoglyceride monoacylglycerols] (MG) into fatty acids and glycerol <ref name="Taschler">[Taschler, U., F. P. W. Radner, C. Heier, R. Schreiber, M. Schweiger, G. Schoiswohl, K. Preiss-Landl, D. Jaeger, B. Reiter, H. C. Koefeler, J. Wojciechowski, C. Theussl, J. M. Penninger, A. Lass, G. Haemmerle, R. Zechner, and R. Zimmermann. "Monoglyceride Lipase Deficiency in Mice Impairs Lipolysis and Attenuates Diet-induced Insulin Resistance." Journal of Biological Chemistry 286.20 (2011): 17467-7477]</ref> .  MGL also terminates the signaling of a primary endocannabinoid, 2-AG <ref name="Savinainen">[Savinainen, Juha R., Megumi Yoshino, Anna Minkkilä, Tapio Nevalainen, and Jarmo T. Laitinen. "Characterization of Binding Properties of Monoglyceride Lipase Inhibitors by a Versatile Fluorescence-based Technique." Analytical Biochemistry 399.1 (2010): 132-34]</ref>. MGL is the main enzyme responsible for hydrolyzing 2-arachidonoylglycerol into arachidonic acid and glycerol ''in vivo'' (Figure 3) <ref name="Bertrand">[ Bertrand, T., F. Augé, J. Houtmann, A. Rak, F. Vallée, V. Mikol, P.f. Berne, N. Michot, D. Cheuret, C. Hoornaert, and M. Mathieu. "Structural Basis for Human Monoglyceride Lipase Inhibition." Journal of Molecular Biology 396.3 (2010): 663-73.]</ref>. One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research.
+Monoglyceride [[:Category:Lipase| Lipase]] (MGL) is part of the α/β hydrolase family,a [[:Category:Serine hydrolase| Serine hydrolase]] (Figure 1), having a <scene name='58/580298/Catalytic_triad/4'>Ser-His-Asp catalytic triad </scene> <ref name="Clemente">[Clemente, J. C., E. Nulton, M. Nelen, M. J. Todd, D. Maguire, C. Schalk-Hihi, L. C. Kuo, S.-P. Zhang, C. M. Flores, and J. K. Kranz. "Screening and Characterization of Human Monoglyceride Lipase Active Site Inhibitors Using Orthogonal Binding and Functional Assays." Journal of Biomolecular Screening 17.5 (2012): 629-40]</ref>. [http://en.wikipedia.org/wiki/Monoacylglycerol_lipase MGL] is present in most cells, providing the rate limiting step for  the hydrolysis of [http://en.wikipedia.org/wiki/Monoglyceride monoacylglycerols] (MG) into fatty acids and glycerol <ref name="Taschler">[Taschler, U., F. P. W. Radner, C. Heier, R. Schreiber, M. Schweiger, G. Schoiswohl, K. Preiss-Landl, D. Jaeger, B. Reiter, H. C. Koefeler, J. Wojciechowski, C. Theussl, J. M. Penninger, A. Lass, G. Haemmerle, R. Zechner, and R. Zimmermann. "Monoglyceride Lipase Deficiency in Mice Impairs Lipolysis and Attenuates Diet-induced Insulin Resistance." Journal of Biological Chemistry 286.20 (2011): 17467-7477]</ref> .  MGL also terminates the signaling of a primary endocannabinoid, 2-arachidonoyl glycerol (2-AG) <ref name="Savinainen">[Savinainen, Juha R., Megumi Yoshino, Anna Minkkilä, Tapio Nevalainen, and Jarmo T. Laitinen. "Characterization of Binding Properties of Monoglyceride Lipase Inhibitors by a Versatile Fluorescence-based Technique." Analytical Biochemistry 399.1 (2010): 132-34]</ref>. MGL is the main enzyme responsible for hydrolyzing 2-arachidonoylglycerol into arachidonic acid and glycerol ''in vivo'' (Figure 3) <ref name="Bertrand">[ Bertrand, T., F. Augé, J. Houtmann, A. Rak, F. Vallée, V. Mikol, P.f. Berne, N. Michot, D. Cheuret, C. Hoornaert, and M. Mathieu. "Structural Basis for Human Monoglyceride Lipase Inhibition." Journal of Molecular Biology 396.3 (2010): 663-73.]</ref>. One of the key features of MGL is the hydrophobic tunnel, which has been suggested to provide a model for drug research (Figure 7).
 ===Metabolic Role===
-Monoglyceride lipase is able to hydrolyze monoacylglycerols into fatty acids and glycerol, which are able to then be used for energy production. MGL degrades sn-1 and 2-MG at identical specific rates as a part of its metabolic role <ref name="Taschler" />.
+Monoglyceride Lipase is involved in energy metabolism through two mechanisms. In the first mechanism of energy metabolism, MGL is able to hydrolyze monoacylglycerols into fatty acids and glycerol, which are able to then be used for energy production <ref name="Taschler" />. The second mechanism involves the degradation of 2-arachidonoyl glycerol (2-AG), which is a common endogenous ligand of cannabinoid receptors, by MGL.  Looking ''in vivo'' of the metabolic role of MGL, MGL deficient mice showed increased monoacylglycerols in adipose tissue, brain, and liver as well as elevated 2-AG levels.  With defective MGL, lipolysis is debilitated and diet-induced insulin resistance is reduced <ref name="Taschler" />.
 ===Component of Endocannabinoid System===