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Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. Lipases are important in digestion, promoting absorption of fats in the intestines. Lipase is primarily found in the pancreas but is also found in the mouth and the stomach. Pancreatic lipase (PDB ID: 1HPL) which is pictured below catalyzes the hydrolysis of triacylglycerols into 2-monoacylglycerols and free fatty acids. Pancreatic liapase consists of two identical chains, totaling 449 residues. | Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. Lipases are important in digestion, promoting absorption of fats in the intestines. Lipase is primarily found in the pancreas but is also found in the mouth and the stomach. Pancreatic lipase (PDB ID: 1HPL) which is pictured below catalyzes the hydrolysis of triacylglycerols into 2-monoacylglycerols and free fatty acids. Pancreatic liapase consists of two identical chains, totaling 449 residues. | ||
| - | == | + | == Structure == |
| - | Pancreatic Lipase Secondary Structure<StructureSection load='1HPL' size='500' side='right' caption='Horse Pancreatic Lipase at 2.3 Angstroms Resolution (PDB ID: 1HPL)' scene=''>The two identical chains of lipase are pictured in blue-gray and green. Lipase has a <scene name='Sandbox_45/Secondary_structure/1'>secondary structure</scene> consisting of 22% alpha helices, which are shown in blue, and 30% beta sheets, which are shown in bright green. The rest of the secondary structure consists of ordered, nonrepetitive structure. Lipase contains two domains. The N-terminal domain is 337 residues long and consists mainly of 3 layer (alpha, beta, alpha) sandwich. The C-terminal domain is 112 residues long and consists primarily of beta sandwich. Lipase also contains six disulfide bonds which are illustrated by the yellow rods. Calcium ions, shown as bright green balls, are also seen interacting with the protein. | + | Pancreatic Lipase Secondary Structure<StructureSection load='1HPL' size='500' side='right' caption='Horse Pancreatic Lipase at 2.3 Angstroms Resolution (PDB ID: 1HPL)' scene=''>The two identical chains of lipase are pictured in blue-gray and green. Lipase has a <scene name='Sandbox_45/Secondary_structure/1'>secondary structure</scene> consisting of 22% alpha helices, which are shown in blue, and 30% beta sheets, which are shown in bright green. The rest of the secondary structure consists of ordered, nonrepetitive structure. Lipase contains two domains. The N-terminal domain is 337 residues long and consists mainly of 3 layer (alpha, beta, alpha) sandwich. The C-terminal domain is 112 residues long and consists primarily of beta sandwich. Lipase also contains six <scene name='Sandbox_45/Disulfide_bonds/3'>disulfide bonds</scene> which are illustrated by the yellow rods. Calcium ions, shown as bright green balls, are also seen interacting with the protein. |
== Hydrophobicity/Hydrophilicity== | == Hydrophobicity/Hydrophilicity== | ||
Revision as of 04:02, 10 November 2011
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| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Contents |
Lipase
Introduction
Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. Lipases are important in digestion, promoting absorption of fats in the intestines. Lipase is primarily found in the pancreas but is also found in the mouth and the stomach. Pancreatic lipase (PDB ID: 1HPL) which is pictured below catalyzes the hydrolysis of triacylglycerols into 2-monoacylglycerols and free fatty acids. Pancreatic liapase consists of two identical chains, totaling 449 residues.
Structure
Pancreatic Lipase Secondary Structure
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Ligand Interaction
Ligand Interaction
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