Sandbox 43: Difference between revisions

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{{template:Oberholser Sandbox Reservation}}
{{template:Oberholser Sandbox Reservation}}


Introduction <StructureSection load='1hpl' size='500' side='right' caption='Structure of Horse Pancreatic Lipase (PDB entry [[1hpl]])' scene=''>Lipase, as its name suggests, is an enzyme responsible for the cleavage of types of lipid molecules. There are different types of lipases, many of which work in similar ways. For instance, Human Pancreatic Lipase, or HPL, splits triglycerides, the main lipids in the human diet, into glycerol and three fatty acids. The structure shown at right is that of Horse Pancreatic Lipase. It consists of two identical subunits, totaling 449 amino acids each.  
Introduction <StructureSection load='1hpl' size='500' side='right' caption='Structure of Horse Pancreatic Lipase (PDB entry [[1hpl]])' scene=''>A subclass of esterases, lipase 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.  
The <scene name='Sandbox_40/Qm_lipase_secondary_structures/1'>secondary structures</scene> of lipase (just one subunit) include 102 residues which create 13 alpha helices, shown in black, and 139 residues involved in beta sheets totaling 28 strands, shown in red. Lipase of course consists of both     
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 <scene name='Sandbox_40/Qm_lipase_secondary_structures/1'>secondary structures</scene> of lipase (just one subunit) include 102 residues which create 13 alpha helices, shown in black, and 139 residues involved in beta sheets totaling 28 strands, shown in red. Lipase of course consists of both     


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