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[[Image:Catalytic_triad.png|right|200|thumb|Catalytic Triad of MGL structure]]
[[Image:Catalytic_triad.png|right|200|thumb|Catalytic Triad of MGL structure]]
====Binding====
====Binding====
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2-AG binds to the catalytic triad and is hydrolyzed. The structure of 2-AG contains a long and flexible aliphatic chain and a polar head that is cleaved. 2-AG is broken down into arachidonic acid and glycerol which makes 2-AG inactive. [[Overall Reaction]]
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2-AG binds to the catalytic triad and is hydrolyzed. The structure of 2-AG contains a long and flexible aliphatic chain and a polar head that is cleaved. 2-AG is broken down into arachidonic acid and glycerol which makes 2-AG inactive. See Overall Reaction.
===Inhibition===
===Inhibition===
Research on MGL is being geared towards inhibiting 2-AG from binding to the catalytic triad and being hydrolyzed. The binding of 2-AG to the catalytic triad can not be inhibited, but it can be extracted before being hydrolyzed. MPD (2-methyl-pentane-2,4-diol)is located at the end of the tunnel where the catalytic triad is at and the tunnel is filled with MPD molecules. MPD being in the same vicinity will extract 2-AG from the triad and the MPD molecule will sit in there in place of 2-AG. This natural inhibition phenomenon is known as interfacial activation.
Research on MGL is being geared towards inhibiting 2-AG from binding to the catalytic triad and being hydrolyzed. The binding of 2-AG to the catalytic triad can not be inhibited, but it can be extracted before being hydrolyzed. MPD (2-methyl-pentane-2,4-diol)is located at the end of the tunnel where the catalytic triad is at and the tunnel is filled with MPD molecules. MPD being in the same vicinity will extract 2-AG from the triad and the MPD molecule will sit in there in place of 2-AG. This natural inhibition phenomenon is known as interfacial activation.

Revision as of 00:18, 25 March 2014

Monoglyceride Lipase (MGL)

Secondary structure of MGL

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