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| - | {{Template:Oberholser Sandbox Reservation}} | + | {{Template:Oberholser_Sandbox_Reservation}} |
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| - | == '''Lipase''' ==
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| | ==Introduction== | | ==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 load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' /> |
| - | | + | <scene name='Sandbox_45/Ak_backbone/1'>Backbone</scene> |
| - | == Secondary Structure==
| + | <scene name='Sandbox_45/Ak_alpha_helix_2/1'>Alpha Helices</scene> |
| - | 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.
| + | <scene name='Sandbox_45/Ak_beta_sheet/1'>Beta Sheet</scene> |
| - | | + | <scene name='Sandbox_45/Ak_alpha_beta_sheet/1'>secondary structure</scene> |
| - | == Hydrophobicity/Hydrophilicity== | + | <scene name='Sandbox_45/Ak_hbonds/1'>Hydrogen Bonds</scene> |
| - | In lipase, there is a relatively equal distribution of <scene name='Sandbox_45/Hydrophobic_residues/2'>hydrophobic residues</scene> and hydrophillc residues. Hydrophobic residues are shown in bright blue when clicking the green link. <scene name='Sandbox_45/Acidic_and_basic_residues/1'>Acidic and basic residues</scene> contribute to the relative hydophilicity of the protein since they can be protonated and deprotonated at varying pH levels, causing a charge to be present. The distribution and number of acidic and basic residues is relatively even.
| + | <scene name='Sandbox_45/Ak_hydrophobic_residues/1'>Hydrophobic residues</scene> |
| - | | + | <scene name='Sandbox_45/Ak_hydrophilic_residues/1'>Hydrophilic residues</scene> |
| - | == Catalytic Function ==
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| - | 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 (N terminal domain) and consist of Ser 152, Asp 172, and His 263. Serine functions to form a covalent bond to the ester, forming a tetrahedral intermediate. Aspartate and histidine function in acid-base catalysis by accepting and donating hydrogen atoms to stabilize the reaction.</StructureSection>
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| - | == Ligand Interaction ==
| + | <scene name='Sandbox_45/Ak_hbonds_actual/1'>The Hydrogen Bonds</scene> |
| - | Ligand Interaction<StructureSection load='1ETH' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1ETH]])' scene=''> <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 directly in the middle of each of the lipase chains.</StructureSection>
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