Sandbox 49

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=Introduction=
=Introduction=
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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. 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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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.
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==Structure==
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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.
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.
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.

Revision as of 01:27, 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.

PDB ID 1hpl

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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 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

Lipase has 449 amino acid resiudes, and 2 domains, the is smaller with 112 residues, and the 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. The secondary structural elements of Lipase, including the 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. The protein is held together by a combination of several factors, the 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 , Lipase has 12 disulfide bonds in all.


References


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