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

Revision as of 03:59, 7 November 2011 by Student (Talk | contribs)
Jump to: navigation, search

>

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 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 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

Structure of HMG-CoA reductase (PDB entry 1HPL)

Drag the structure with the mouse to rotate

Ligand Interaction Pancreatic lipase is shown here in a complex with the coenzyme colipase, which enhances lipase's function. The two identical lipase chains are pictured in pink and blue. The two identical chains of colipase are pictured in yellow and green. Three ligands are shown in association with the two lipase chains. Two calcium ions are shown in green as space-filling balls. Beta-mercaptoethanol is also shown as yellow, grey, and red balls. Lastly, (hydroxyethyloxy)tri(ethyloxy)octane is pictured as the larger grey, white, and red ball cluster.

Personal tools