Sandbox 43

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. Horse Pancreatic Lipase Introduction <StructureSection load='1hpl' size='500' side='right' caption='Structure of Horse Pancreatic Lipase (PDB entry 1hpl)' scene=>A subclass of esterases, pancreatic lipase (EC 3.1.1.3) is an enzyme that catalyzes the hydrolysis and formation of lipids. While produced in the pancreas, it is also present in the stomach and mouth. Due to its effective ester bond hydrolysis of lipids, lipase is essential for fat digestion, breaking lipids into monoglycerides and single fatty acids. Structure The quaternary structure of horse pancreatic lipase (as featured right) contains two molecules which each contain 449 amino acid residues, 705 water molecules, and 2 calcium ions. These two identical molecules are connected by a two-fold symmetry axis. The secondary structure of lipase is composed of 102 residues that constitute 13 alpha helices (22% helical) and 139 residues that constitute 28 beta sheet strands (30% beta sheets). The hydrophobic regions of lipase are shown in yellow. Most of the hydrophobic regions are buried deep in the molecule so as to reduce interactions with water. The most prominent ligand involved in the structure of lipase is the calcium ion . This ion has been shown to promote the folding of lipase into its active dimer state.