|
|
| (29 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | {{Template:Oberholser_Sandbox_Reservation}}<applet load='1hpl' size='300' frame='true' align='right' caption='<scene name='caption'/> | + | <!-- PLEASE DO NOT DELETE THIS TEMPLATE --> |
| - | | + | {{Template:Oberholser_Sandbox_Reservation}} |
| - | =Introduction=
| + | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> |
| - | Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase is an important enzyme that is manufactured in the pancreas and that aids in the process of digestion, the particular type modeled here is horse pancreatic lipase.
| + | <Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here'/> |
| - | | + | <scene name='Sandbox_49/Ak_backbone/1'>Backbone</scene> |
| - | ==Structure==
| + | <scene name='Sandbox_49/Ak_alpha_helices/1'>Alpha_helices</scene> |
| - | Lipase has 449 amino acid resiudes, and 2 domains, the <scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene> is smaller with 112 residues, and the <scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domain</scene> consists of 337 residues. Notice that each of these domains consist of 2 identical subunits. Lipase has an a chain and a b chain that each respectively contain 1 of the subunits of the C Terminal Domain and 1 of the subunits of the N terminal domains, all 4 parts come together to form the fully functional enzyme.
| + | <scene name='Sandbox_49/Ak_beta_sheets/1'>Beta_sheets</scene> |
| - | The secondary structural elements of Lipase, including the <scene name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene> that make up 30 percent of the amino acid chain, and involving 139 residues as well as the <scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene> that make up 22 percent and 102 residues characterize the structure of the protein. The protein is held together by a combination of several factors, the <scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene> certainly make a difference as one might expect, since all proteins generally fold to shield these from interaction with water, the cysteine residues that Lipase has also play a major role since they form <scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene>, Lipase has 12 disulfide bonds in all. Lipase also has a <scene name='Sandbox_49/Ca_ligands/1'>Ca Ligand</scene> that noncovalently binds to residues: Glu 187, Arg 190, Asp 192, Asp 195. There is one Calcium ion bound per chain in the enzyme.
| + | <scene name='Sandbox_49/Ak_secondary_structures/1'>secondary_structure</scene> |
| - | The <scene name='Sandbox_49/Lipase_active_sites_test/1'>Lipase Active Sites</scene> catalytic groups are protected by a flap that folds over the are when a substrate is bound, aiding in the catalytic function of the enzyme.
| + | <scene name='Sandbox_49/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene> |
| - | | + | <scene name='Sandbox_49/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> |
| - | | + | |
| - | ==References==
| + | |
| - | *http://www.brenda-enzymes.org/php/result_flat.php4?ecno=3.1.1.3
| + | |
| - | *http://enzyme.expasy.org/cgi-bin/enzyme/enzyme-search-ec
| + | |
| - | *http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL
| + | |
| - | *Fundamentals of Biochemistry, Voet
| + | |
| - | *
| + | |
| - | *
| + | |
| - | *
| + | |
| - | *
| + | |
| - | | + | |
| - | | + | |
| - | <scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene> | + | |
| - | | + | |
| - | <scene name='Sandbox_49/Lipase_active_sites_test/1'>Lipase Active Sites</scene> | + | |
| - | | + | |
| - | <scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene> | + | |
| - | | + | |
| - | <scene name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/Turns_1/1'>Turns</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domains</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/Ca_ligands/1'>Ca Ligands</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/Lipase_inhibitor/1'>Lipase Inhibitor</scene>
| + | |
| - | | + | |
| - | <scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene> | + | |