Sandbox reserved 915: Difference between revisions

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Taschler et al. looked at the role of MGL in energy metabolism, finding that MGL deficiency in animals led to the buildup of 2-AG (Taschler et al. 2011).

===Inhibition of MGL===

Studies have shown that N-arachidonylmaleimide (NAM) inhibits MGL by reacting with the amino acid Cys252. This Cysteine is buried in the active site near the catalytic serine. This inhibition can be explained by a steric clash between the inhibitor and the natural ligand. There is also a possibility of conformational changes upon the binding of the cysteine that would lead to an inactive form of MGL.

Studies have shown that N-arachidonylmaleimide (NAM) inhibits MGL by reacting with the amino acid <scene name='58/580298/Cys252/1'>Cys252</scene>. This Cysteine is buried in the active site near the catalytic serine. This inhibition can be explained by a steric clash between the inhibitor and the natural ligand. There is also a possibility of conformational changes upon the binding of the cysteine that would lead to an inactive form of MGL.

MGL is also inhibited by being in complex with SAR629 that is covalently bound to the catalytic Ser132. SAR629 adopts a Y shape and interacts with the MGL by hydrophobic interactions, with a few polar interactions as well. With SAR629 interacting with the catalytic triad it inhibits the triad from breaking down 2-AG and it interacting with MGL makes it inactive.

==Structure==

Sandbox reserved 915: Difference between revisions

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@@ Line 10: / Line 10: @@
 Taschler et al. looked at the role of MGL in energy metabolism, finding that MGL deficiency in animals led to the buildup of 2-AG (Taschler et al. 2011).
 ===Inhibition of MGL===
-Studies have shown that N-arachidonylmaleimide (NAM) inhibits MGL by reacting with the amino acid Cys252. This Cysteine is buried in the active site near the catalytic serine. This inhibition can be explained by a steric clash between the inhibitor and the natural ligand. There is also a possibility of conformational changes upon the binding of the cysteine that would lead to an inactive form of MGL.
+Studies have shown that N-arachidonylmaleimide (NAM) inhibits MGL by reacting with the amino acid <scene name='58/580298/Cys252/1'>Cys252</scene>. This Cysteine is buried in the active site near the catalytic serine. This inhibition can be explained by a steric clash between the inhibitor and the natural ligand. There is also a possibility of conformational changes upon the binding of the cysteine that would lead to an inactive form of MGL.
 MGL is also inhibited by being in complex with SAR629 that is covalently bound to the catalytic Ser132. SAR629 adopts a Y shape and interacts with the MGL by hydrophobic interactions, with a few polar interactions as well. With SAR629 interacting with the catalytic triad it inhibits the triad from breaking down 2-AG and it interacting with MGL makes it inactive.
 ==Structure==