Sandbox 49
From Proteopedia
(Difference between revisions)
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=Introduction= | =Introduction= | ||
| + | Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. 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. The secondary structural elements of Lipase, including the 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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| + | ==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 | ||
| + | * | ||
| + | * | ||
| + | * | ||
| + | * | ||
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<scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene> | <scene name='Sandbox_49/Lipase_hydrohpobic_residues/1'>hydrophobic residues</scene> | ||
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<scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domains</scene> | <scene name='Sandbox_49/N_terminal_domain_1/1'>N Terminal Domains</scene> | ||
| - | |||
| - | <scene name='Sandbox_49/C_terminal_domains/1'>C Terminal Domains</scene> | ||
<scene name='Sandbox_49/Ca_ligands/1'>Ca Ligands</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/Lipase_inhibitor/1'>Lipase Inhibitor</scene> | ||
| + | |||
| + | <scene name='Sandbox_49/Disulfide_bonds/1'>Disulfide Bonds</scene> | ||
Revision as of 01:16, 15 November 2011
| 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. |
|
Introduction
Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase has 449 amino acid resiudes, and 2 domains, the is smaller with 112 residues, and the consists of 337 residues. The secondary structural elements of Lipase, including the 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 that make up 22 percent and 102 residues characterize the structure of the protein.
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
