This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox 45
From Proteopedia
| Line 2: | Line 2: | ||
{{Template:Oberholser Sandbox Reservation}} | {{Template:Oberholser Sandbox Reservation}} | ||
<!--- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!--- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| + | |||
| + | Lipase is a hydrolase that catalyzes the breakdown of lipids. 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 which is pictured below catalyzes the hydrolysis of triacylglycerols at the 1 and 3 positions to from 1,2-diacylglycerols and 2-acylglycerols. Pancreatic liapase consists of two identical chains, totaling 449 residues. | ||
Lipase Secondary Structure<StructureSection load='1HPL' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1HPL]])' scene=''>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 also contains six disulfide bonds which are illustrated by the yellow rods. <scene name='Sandbox_45/Hydrophobic_residues/2'>Hydrophobic Residues</scene> Lipase contains three important <scene name='Sandbox_45/Active_site/5'>active site residues</scene> which are highlighted in yellow. These three catalytic residues are all located in the A chain and consist of Ser 152, Asp 172, and His 263. | Lipase Secondary Structure<StructureSection load='1HPL' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1HPL]])' scene=''>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 also contains six disulfide bonds which are illustrated by the yellow rods. <scene name='Sandbox_45/Hydrophobic_residues/2'>Hydrophobic Residues</scene> Lipase contains three important <scene name='Sandbox_45/Active_site/5'>active site residues</scene> which are highlighted in yellow. These three catalytic residues are all located in the A chain and consist of Ser 152, Asp 172, and His 263. | ||
Revision as of 02:06, 7 November 2011
>
| 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. |
Lipase is a hydrolase that catalyzes the breakdown of lipids. 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 which is pictured below catalyzes the hydrolysis of triacylglycerols at the 1 and 3 positions to from 1,2-diacylglycerols and 2-acylglycerols. Pancreatic liapase consists of two identical chains, totaling 449 residues.
| |||||||||||
