Sandbox 47: Difference between revisions
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{{Template:Oberholser_Sandbox_Reservation}} | {{Template:Oberholser_Sandbox_Reservation}} | ||
== '''Introduction''' == | == '''Introduction''' == | ||
Pancreatic lipase (EC 3.1.1.3) is an esterase enzyme secreted from the pancreas. It breaks down lipids in the digestive system | Pancreatic lipase (EC 3.1.1.3) is an esterase enzyme secreted from the pancreas. It breaks down lipids in the digestive system by ester hydrolysis. It converts its triglyceride substrates to monoglycerides and free acids by ester hydrolysis. <ref>"Pancreatic lipase". Wikipedia: The Free Encyclopedia. 7 Nov 2011 [http://en.wikipedia.org/wiki/Pancreatic_lipase]</ref> Pancreatic triglyceride lipase is critical for the efficient absorption of dietary fats.<ref>"Colipase". Wikipedia: The Free Encyclopedia. 5 July 2011 [http://en.wikipedia.org/wiki/Colipase]</ref> | ||
<StructureSection load='1hpl' size='500' frame='true' align='right' scene='Sandbox_47/Liipase/1' caption='Lipase' /> | <StructureSection load='1hpl' size='500' frame='true' align='right' scene='Sandbox_47/Liipase/1' caption='Lipase' /> | ||
== '''Structure''' == | == '''Structure''' == | ||
Horse pancreatic lipase (PDB ID-1hpl) is an asymmetrical molecule that consists of two subunits, each of which contain 449 amino acids and 705 well-defined water molecules. The two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>, interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. The subunits are related by a 2-fold non-crystallographic symmetry axis. Lipase also binds two <scene name='Sandbox_47/Lipase_calcium/2'>calcium ions</scene> as ligands through a variety of <scene name='Sandbox_47/Calciumcontacts/4'>contacts</scene>. Its <scene name='Sandbox_47/Lipasesecondarystructures/1'>secondary structure</scene> consists of 22% <scene name='Sandbox_47/Lipase_helix/2'>helices</scene> and 30% <scene name='Sandbox_47/Lipase_sheet/2'>beta sheets</scene>. It contains both <scene name='Sandbox_47/Lipase_hydrophobicres/2'>hydrophobic</scene> (red) and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene> (blue). The overall molecular structure of horse lipase has two well-defined domains. The <scene name='Sandbox_47/Nterminal/1'>N-terminal</scene> domain (residues 1-336) contains the <scene name='Sandbox_47/Activesite/4'>active site</scene> and has a typical alpha/beta hydrolase fold topology. The active site contains a catalytic triad (Ser-152, Asp-176, and His-263) that closely resembles that of serine proteases. The N-terminal domain also contains a <scene name='Sandbox_47/Lid/1'>"lid"</scene> that blocks solvent from entering the active site. The <scene name='Sandbox_47/Cterminal/1'>C-terminal</scene> domain (residues (337-449), for colipase binding, has a beta-sheet sandwich topology.<ref>Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. 1994. Horse pancreatic lipase. J. mol Biol. 238: 709-732.</ref> | Horse pancreatic lipase (PDB ID-1hpl) is an asymmetrical molecule that consists of two subunits, each of which contain 449 amino acids and 705 well-defined water molecules. The two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>, interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. The subunits are related by a 2-fold non-crystallographic symmetry axis. Lipase also binds two <scene name='Sandbox_47/Lipase_calcium/2'>calcium ions</scene> as ligands through a variety of <scene name='Sandbox_47/Calciumcontacts/4'>contacts</scene>. Its <scene name='Sandbox_47/Lipasesecondarystructures/1'>secondary structure</scene> consists of 22% <scene name='Sandbox_47/Lipase_helix/2'>helices</scene> and 30% <scene name='Sandbox_47/Lipase_sheet/2'>beta sheets</scene>. It contains both <scene name='Sandbox_47/Lipase_hydrophobicres/2'>hydrophobic</scene> (red) and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene> (blue). The overall molecular structure of horse lipase has two well-defined domains. The <scene name='Sandbox_47/Nterminal/1'>N-terminal</scene> domain (residues 1-336) contains the <scene name='Sandbox_47/Activesite/4'>active site</scene> and has a typical alpha/beta hydrolase fold topology. The active site contains a catalytic triad (Ser-152, Asp-176, and His-263) that closely resembles that of serine proteases. The N-terminal domain also contains a <scene name='Sandbox_47/Lid/1'>"lid"</scene> that blocks solvent from entering the active site. The <scene name='Sandbox_47/Cterminal/1'>C-terminal</scene> domain (residues (337-449), for colipase binding, has a beta-sheet sandwich topology.<ref>Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. 1994. Horse pancreatic lipase. J. mol Biol. 238: 709-732.</ref> | ||
