Sandbox 40: Difference between revisions

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The consistency of residues between variations of lipases can be described as the <scene name='Sandbox_40/Evolutionary_conservation/1'>evolutionary conservation</scene> of the protein. As it can be observed from the conservation of individual residues, the residues near the active site and close to the calcium ligand have the highest average conservation. The conservation of residues becomes more variable the farther away from each active site.

=Optimization of Action=

In order for the action of Pancreatic Lipase to be optimized in vivo, a coenzyme called colipase must be secreted by the pancreas and activated by intestinal trypsin. Colipase prevents bile salts from inhibiting the regular action of Pancreatic Lipase. Colipase binds to the C-terminal of a subunit of Pancreatic Lipase, stabilising the active conformation. Shown here is <scene name='Sandbox_40/Colipase_2/1'>colipase</scene> bound to a subunit of Pancreatic Lipase. This view shows the many <scene name='Sandbox_40/Contacts_colipase/1'>contacts</scene> between colipase and Pancreatic Lipase. The pancreatic lipase - colipase complex structure and mechanism was discovered through the use of an <scene name='Sandbox_40/Colipase/1'>inhibitor</scene>, a C11 alkyl phosphonate. The C11 alkyl group of the inhibitor acts as a fatty acid of a triglyceride would, ~~interacting with~~ the ~~hydrophobic rift leading to~~ the ~~active site~~.

In order for the action of Pancreatic Lipase to be optimized in vivo, a coenzyme called colipase must be secreted by the pancreas and activated by intestinal trypsin. Colipase prevents bile salts from inhibiting the regular action of Pancreatic Lipase. Colipase binds to the C-terminal of a subunit of Pancreatic Lipase, stabilising the active conformation. Shown here is <scene name='Sandbox_40/Colipase_2/1'>colipase</scene> bound to a subunit of Pancreatic Lipase. This view shows the many <scene name='Sandbox_40/Contacts_colipase/1'>contacts</scene> between colipase and Pancreatic Lipase. The pancreatic lipase - colipase complex structure and mechanism was discovered through the use of an <scene name='Sandbox_40/Colipase/1'>inhibitor</scene>, a C11 alkyl phosphonate. The C11 alkyl group of the inhibitor acts as a fatty acid of a triglyceride would, but cannot be cleaved from the phosphate head of the phosphonate. Seen in this scene is the lipase - colipase complex with mutliple phosphonate inhibitors.

=References=

Sandbox 40: Difference between revisions

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 The consistency of residues between variations of lipases can be described as the <scene name='Sandbox_40/Evolutionary_conservation/1'>evolutionary conservation</scene> of the protein. As it can be observed from the conservation of individual residues, the residues near the active site and close to the calcium ligand have the highest average conservation.  The conservation of residues becomes more variable the farther away from each active site.
 =Optimization of Action=
-In order for the action of Pancreatic Lipase to be optimized in vivo, a coenzyme called colipase must be secreted by the pancreas and activated by intestinal trypsin.  Colipase prevents bile salts from inhibiting the regular action of Pancreatic Lipase.  Colipase binds to the C-terminal of a subunit of Pancreatic Lipase, stabilising the active conformation. Shown here is <scene name='Sandbox_40/Colipase_2/1'>colipase</scene> bound to a subunit of Pancreatic Lipase.  This view shows the many <scene name='Sandbox_40/Contacts_colipase/1'>contacts</scene> between colipase and Pancreatic Lipase.   The pancreatic lipase - colipase complex structure and mechanism was discovered through the use of an <scene name='Sandbox_40/Colipase/1'>inhibitor</scene>, a C11 alkyl phosphonate.  The C11 alkyl group of the inhibitor acts as a fatty acid of a triglyceride would, interacting with the hydrophobic rift leading to the active site.
+In order for the action of Pancreatic Lipase to be optimized in vivo, a coenzyme called colipase must be secreted by the pancreas and activated by intestinal trypsin.  Colipase prevents bile salts from inhibiting the regular action of Pancreatic Lipase.  Colipase binds to the C-terminal of a subunit of Pancreatic Lipase, stabilising the active conformation. Shown here is <scene name='Sandbox_40/Colipase_2/1'>colipase</scene> bound to a subunit of Pancreatic Lipase.  This view shows the many <scene name='Sandbox_40/Contacts_colipase/1'>contacts</scene> between colipase and Pancreatic Lipase.   The pancreatic lipase - colipase complex structure and mechanism was discovered through the use of an <scene name='Sandbox_40/Colipase/1'>inhibitor</scene>, a C11 alkyl phosphonate.  The C11 alkyl group of the inhibitor acts as a fatty acid of a triglyceride would, but cannot be cleaved from the phosphate head of the phosphonate.  Seen in this scene is the lipase - colipase complex with mutliple phosphonate inhibitors.
 =References=
 <references />