Sandbox 49

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{{Template:Oberholser_Sandbox_Reservation}}<applet load='1hpl' size='300' frame='true' align='right' caption='<scene name='caption'/>
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{{Template:Oberholser_Sandbox_Reservation}}
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=Introduction=
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Lipases represent a critical class of enzymes that functions in the breakdown of triacylglycerides. Produced by the pancreas, lipase catalyzes the hydrolysis of triacylglyercols at their 1 and 3 carbons, resulting the in the production of 2-monoacylglycerols and free fatty acids. Modeled here is horse pancreatic lipase.
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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here'/>
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<scene name='Sandbox_49/Ak_backbone/1'>Backbone</scene>
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==Structure==
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<scene name='Sandbox_49/Ak_alpha_helices/1'>Alpha_helices</scene>
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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.
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<scene name='Sandbox_49/Ak_beta_sheets/1'>Beta_sheets</scene>
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<scene name='Sandbox_49/Ak_secondary_structures/1'>secondary_structure</scene>
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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.
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<scene name='Sandbox_49/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene>
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<scene name='Sandbox_49/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene>
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Important for the tertiary structure of the protein, are several different factors that function to hold each of the domains together in the proper orientation, 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.
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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.
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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.
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==References==
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*http://www.brenda-enzymes.org/php/result_flat.php4?ecno=3.1.1.3
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*http://enzyme.expasy.org/cgi-bin/enzyme/enzyme-search-ec
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*http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL
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*Fundamentals of Biochemistry, Voet
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*http://www.uniprot.org/uniprot/P29183
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*http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/MACiE/entry/displayStructure.pl?id=M0218
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*
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*
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<scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene>
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<scene name='Sandbox_49/Lipase_active_sites_final/1'>Lipase active sites</scene>
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<scene name='Sandbox_49/Alpha_helices_1/1'>Alpha Helices</scene>
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<scene name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene>
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<scene name='Sandbox_49/Turns_1/1'>Turns</scene>
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<scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domains</scene>
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<scene name='Sandbox_49/Ca_ligands/1'>Ca Ligands</scene>
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<scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene>
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<scene name='Sandbox_49/Lipase_inhibitor/1'>Lipase Inhibitor</scene>
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<scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene>
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Current revision

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.

Adenylate Kinase

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