Sandbox 40: Difference between revisions
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=Optimization of Action= | =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/1'>Colipase</scene> bonded 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. | 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/1'>Colipase</scene> bonded 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. | ||
=Inhibition= | |||
The Pancreatic Lipase - Colipase complex structure was identified and its mechanism of action analyzed by the introduction of an inhibitor, a C11 Alkyl Phosponate. The <scene name='Sandbox_40/Inhibition/1'>inhibitor binds</scene> to the lipase - colipase complex similar to the way a triglyceride would. The C11 alkyl group mimics one of the fatty acid groups of a triglyceride and interacts with the hydrophobic groove leading to the active site. | |||
=References= | =References= | ||
<references /> | <references /> | ||
