Sandbox 49: Difference between revisions

Line 12:

==Lipase Active Sites==

The Lipase ~~Active Sites~~ consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site, the open lid is stabilized by the formation of hydrogen bonds to neighboring residues. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme.

The <scene name='Sandbox_49/Lipase_active_sites_final/1'>Lipase active sites</scene> consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site, the open lid is stabilized by the formation of hydrogen bonds to neighboring residues. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme.

==Mechanism==

Line 34:

==Inhibition and Activation==

C11 alkyl phosphate is an effective inhibitor of pancreatic lipase, it was synthesized in an attempt to gain a better understanding of the enzyme’s active site. The inhibitor’s alkyl chain fits into the hydrophobic groove of the active site’s catalytic triad and covalently binds to Ser 152, but instead of reacting like the normal triacylglyceride substrate the inhibitor does not react and stays bound, effectively destroying the ability of the enzyme to function.

Bile salts are steroids important for further degradation of the triacylglycerides processed by pancreatic lipase, however they are also inhibitors of the lipase as well. To prevent this inhibition the cofactor colipase is vital. Colipase is secreted by the pancreas in its inactive form procolipase, upon activation the protein binds to the noncatalytic C terminal arm of Lipase to activate the protein.

Sandbox 49: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 12: / Line 12: @@
 ==Lipase Active Sites==
-The Lipase Active Sites consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site, the open lid is stabilized by the formation of hydrogen bonds to neighboring residues. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme.
+The <scene name='Sandbox_49/Lipase_active_sites_final/1'>Lipase active sites</scene> consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site, the open lid is stabilized by the formation of hydrogen bonds to neighboring residues. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme.
 ==Mechanism==
@@ Line 34: / Line 34: @@
 ==Inhibition and Activation==
 C11 alkyl phosphate is an effective inhibitor of pancreatic lipase, it was synthesized in an attempt to gain a better understanding of the enzyme’s active site. The inhibitor’s alkyl chain fits into the hydrophobic groove of the active site’s catalytic triad and covalently binds to Ser 152, but instead of reacting like the normal triacylglyceride substrate the inhibitor does not react and stays bound, effectively destroying the ability of the enzyme to function.
 Bile salts are steroids important for further degradation of the triacylglycerides processed by pancreatic lipase, however they are also inhibitors of the lipase as well. To prevent this inhibition the cofactor colipase is vital. Colipase is secreted by the pancreas in its inactive form procolipase, upon activation the protein binds to the noncatalytic C terminal arm of Lipase to activate the protein.