Sandbox 51: Difference between revisions

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Pancreatic lipase 1hpl (EC 3.1.1.3) is a an enzyme involved with the digestion and absorption of triacylglycerols (fats) in the intestine. It is secreted by the pancreas into the duodenum where it participates in the initial stages of breaking down fats <ref>Voet, D.,etc. "Fundamentals of Biochemistry: Life at the Molecular Level" John Wiley and Sons, Inc: New Jersey, 2008.</ref>

==Structure==

1hpl is the horse pancreatic lipase enzyme that is thought to have a similar structure and function to the human pancreatic lipase. The <scene name='Sandbox_51/Lipase_crystal_structure/1'> Crystal Structure</scene> of the human pancreatic lipase has not yet been published. Lipase has two <scene name='Sandbox_51/Lipase_crystal_structure/3'>individual molecules</scene> of 449 amino acid residues interacting with one <scene name='Sandbox_51/Ligand_position/2'>Calcium Ligand</scene> each. The calcium ion <scene name='Sandbox_51/Calcium_orientation/2'>orientation</scene> shows that the molecule is located between acidic residues Arg, Asp and Glu. The enzyme has 13 alpha helices (pink) and 22 beta sheets (yellow)per subunit as displayed in the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene>. The molecule has a varying degree of <scene name='Sandbox_51/Lipase_crystal_structure/4'>polar/hydrophobic residues</scene> interspersed within the molecules <ref>Bourne, Y., etc. "Horse pancreatic lipase..."(1994) J.Mol.Biol. 238: 709-732 [http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL]</ref>. This is important because the enzyme actively digests at the lipid-water interface of the fatty micelles, requiring stability in both polar and non polar environments <ref>Fundamentals of Biochemistry...</ref>. The enzyme has

1hpl is the horse pancreatic lipase enzyme that is thought to have a similar structure and function to the human pancreatic lipase. The <scene name='Sandbox_51/Lipase_crystal_structure/1'> Crystal Structure</scene> of the human pancreatic lipase has not yet been published. Lipase has two <scene name='Sandbox_51/Lipase_crystal_structure/3'>individual molecules</scene> of 449 amino acid residues interacting with one <scene name='Sandbox_51/Ligand_position/2'>Calcium Ligand</scene> each. The calcium ion <scene name='Sandbox_51/Calcium_orientation/2'>orientation</scene> shows that the molecule is located between acidic residues Arg, Asp and Glu. The enzyme has 13 alpha helices (pink) and 22 beta sheets (yellow)per subunit as displayed in the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene> <ref>Egloff, M.P., etc. "The 2.46 angstroms resolution structure of the pancreatic lipase colipase complex inhibited by a C11 alkyl phosphonate."(1995) J. Biochemistry 34: 2751-2762 [http://www.pdb.org/pdb/explore/explore.do?structureId=1lpb]</ref>. The molecule has a varying degree of <scene name='Sandbox_51/Lipase_crystal_structure/4'>polar/hydrophobic residues</scene> interspersed within the molecules <ref>Bourne, Y., etc. "Horse pancreatic lipase..."(1994) J.Mol.Biol. 238: 709-732 [http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL]</ref>. This is important because the enzyme actively digests at the lipid-water interface of the fatty micelles, requiring stability in both polar and non polar environments <ref>Fundamentals of Biochemistry...</ref>. The enzyme has

<scene name='Sandbox_51/Nc_terminal/1'>two domain</scene> of various composition specific for certain interaction, an N-terminal (blue) and a C-terminal (red). In the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene>, the N-terminal domain has the hydrolase alpha/beta folding structure, consisting of an alpha-beta sheet consisting of 8 strands connected by helices. The C-terminal domain (enzyme colipase binds) has a beta-sheet sand which folding pattern <ref>Horse pancreatic lipase...</ref> The <scene name='Sandbox_51/Active_site/3'>active site</scene> of the lipase molecule is found in the N-terminal domain (residues 1-336) and contains a <scene name='Sandbox_51/Catalytic_tria/1'>catalytic triad</scene> consisting of a Ser-His-Arg for the ester hydrolysis reaction (similar to that of a serine protease). The active site is covered by a 25-residue helical 'lid' blocking the binding site, unless appropriate conditions <ref>Fundamentals of Biochemistry...</ref>.

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 Pancreatic lipase 1hpl (EC 3.1.1.3)  is a an enzyme involved with the digestion and absorption of triacylglycerols (fats) in the intestine.  It is secreted by the pancreas into the duodenum where it participates in the initial stages of breaking down fats <ref>Voet, D.,etc. "Fundamentals of Biochemistry: Life at the Molecular Level" John Wiley and Sons, Inc: New Jersey, 2008.</ref>
 ==Structure==
-hpl is the horse pancreatic lipase enzyme that is thought to have a similar structure and function to the human pancreatic lipase.  The  <scene name='Sandbox_51/Lipase_crystal_structure/1'> Crystal Structure</scene> of the human pancreatic lipase has not yet been published.   Lipase has two <scene name='Sandbox_51/Lipase_crystal_structure/3'>individual molecules</scene> of 449 amino acid residues interacting with one <scene name='Sandbox_51/Ligand_position/2'>Calcium Ligand</scene> each.  The calcium ion <scene name='Sandbox_51/Calcium_orientation/2'>orientation</scene> shows that the molecule is located between acidic residues Arg, Asp and Glu.  The enzyme has 13 alpha helices (pink) and 22 beta sheets (yellow)per subunit as displayed in the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene>.  The molecule has a varying degree of <scene name='Sandbox_51/Lipase_crystal_structure/4'>polar/hydrophobic residues</scene> interspersed within the molecules <ref>Bourne, Y., etc. "Horse pancreatic lipase..."(1994) J.Mol.Biol. 238: 709-732 [http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL]</ref>.  This is important because the enzyme actively digests at the lipid-water interface of the fatty micelles, requiring stability in both polar and non polar environments <ref>Fundamentals of Biochemistry...</ref>. The enzyme has
+hpl is the horse pancreatic lipase enzyme that is thought to have a similar structure and function to the human pancreatic lipase.  The  <scene name='Sandbox_51/Lipase_crystal_structure/1'> Crystal Structure</scene> of the human pancreatic lipase has not yet been published.   Lipase has two <scene name='Sandbox_51/Lipase_crystal_structure/3'>individual molecules</scene> of 449 amino acid residues interacting with one <scene name='Sandbox_51/Ligand_position/2'>Calcium Ligand</scene> each.  The calcium ion <scene name='Sandbox_51/Calcium_orientation/2'>orientation</scene> shows that the molecule is located between acidic residues Arg, Asp and Glu.  The enzyme has 13 alpha helices (pink) and 22 beta sheets (yellow)per subunit as displayed in the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene> <ref>Egloff, M.P., etc. "The 2.46 angstroms resolution structure of the pancreatic lipase colipase complex inhibited by a C11 alkyl phosphonate."(1995) J. Biochemistry 34: 2751-2762 [http://www.pdb.org/pdb/explore/explore.do?structureId=1lpb]</ref>.  The molecule has a varying degree of <scene name='Sandbox_51/Lipase_crystal_structure/4'>polar/hydrophobic residues</scene> interspersed within the molecules <ref>Bourne, Y., etc. "Horse pancreatic lipase..."(1994) J.Mol.Biol. 238: 709-732 [http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL]</ref>.  This is important because the enzyme actively digests at the lipid-water interface of the fatty micelles, requiring stability in both polar and non polar environments <ref>Fundamentals of Biochemistry...</ref>. The enzyme has
 <scene name='Sandbox_51/Nc_terminal/1'>two domain</scene> of various composition specific for certain interaction, an N-terminal (blue) and a C-terminal (red).  In the <scene name='Sandbox_51/Secondary_structure/2'>secondary structure</scene>, the N-terminal domain has the hydrolase alpha/beta folding structure, consisting of an alpha-beta sheet consisting of 8 strands connected by helices. The C-terminal domain (enzyme colipase binds) has a beta-sheet sand which folding pattern <ref>Horse pancreatic lipase...</ref> The <scene name='Sandbox_51/Active_site/3'>active site</scene> of the lipase molecule is found in the N-terminal domain (residues 1-336) and contains a <scene name='Sandbox_51/Catalytic_tria/1'>catalytic triad</scene> consisting of a Ser-His-Arg for the ester hydrolysis reaction (similar to that of a serine protease).  The active site is covered by a 25-residue helical 'lid' blocking the binding site, unless appropriate conditions <ref>Fundamentals of Biochemistry...</ref>.