Sandbox 45: Difference between revisions

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Note: Clicking on any link generated in first glance causes strange things to happen when clicking on some of the other green links such as addition or removal of some disulfide bonds or atoms in space or removal of the coloration of some other links. Also certain parts of the image that are supposed to be transparent are no longer so. There seems to be nothing able to be done about this issue. So after viewing the subunit contacts, hydrogen bonding, scene cysteine scene, the salt bridge scene, the first calcium ion interaction scene ("four residues"), and the van der waals interaction scene please refresh the page as that seems to allow the other links to work properly again.

==Introduction==

Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. Lipases are important in digestion, promoting absorption of fats in the intestines. Lipase is primarily found in the pancreas but is also found in the mouth and the stomach. Pancreatic lipase (PDB ID: 1HPL) which is pictured below is a carboxylic ester hydrolase. It is ~~further classified as a~~ triacylglycerol lipase (E.C. 3.1.1.3). The ~~general~~ reaction catalyzed by this ~~class of enzymes~~ is shown below. [[Image:Picture 1.png]]

Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids. Lipases are important in digestion, promoting absorption of fats in the intestines. Lipase is primarily found in the pancreas but is also found in the mouth and the stomach. Pancreatic lipase (PDB ID: 1HPL) which is pictured below is a carboxylic ester hydrolase. It is also commonly called pancreatic triacylglycerol lipase and its enzyme class number is E.C. 3.1.1.3 <ref name="1HPL PDB SUM">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1hpl&template=main.html] 1HPL PDB SUM </ref>. The reaction catalyzed by this enzyme is shown below. [[Image:Picture 1.png]]

~~Pancreatic lipase specifically catalyzes the hydrolysis of triacylglycerols into~~ 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. Pancreatic liapase is a 50 kDa protein, consisting of two identical, 449 residue chains <ref name= "1HPL PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL] 1HPL PDB</ref>. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. It wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the focus and many scientists have worked to further this.

Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. Pancreatic liapase is a 50 kDa protein, consisting of two identical, 449 residue chains <ref name= "1HPL PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL] 1HPL PDB</ref>. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. It wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the focus and many scientists have worked to further this.

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@@ Line 6: / Line 6: @@
 Note:  Clicking on any link generated in first glance causes strange things to happen when clicking on some of the other green links such as addition or removal of some disulfide bonds or atoms in space or removal of the coloration of some other links.  Also certain parts of the image that are supposed to be transparent are no longer so.  There seems to be nothing able to be done about this issue.  So after viewing the subunit contacts, hydrogen bonding, scene cysteine scene, the salt bridge scene, the first calcium ion interaction scene ("four residues"), and the van der waals interaction scene please refresh the page as that seems to allow the other links to work properly again.
 ==Introduction==
-Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids.  Lipases are important in digestion, promoting absorption of fats in the intestines.  Lipase is primarily found in the pancreas but is also found in the mouth and the stomach.  Pancreatic lipase (PDB ID:  1HPL) which is pictured below is a carboxylic ester hydrolase.  It is further classified as a triacylglycerol lipase (E.C. 3.1.1.3).  The general reaction catalyzed by this class of enzymes is shown below.  [[Image:Picture 1.png]]
+Lipase is a hydrolase that catalyzes the breakdown of lipids by hydrolyzing the esters of fatty acids.  Lipases are important in digestion, promoting absorption of fats in the intestines.  Lipase is primarily found in the pancreas but is also found in the mouth and the stomach.  Pancreatic lipase (PDB ID:  1HPL) which is pictured below is a carboxylic ester hydrolase.  It is also commonly called pancreatic triacylglycerol lipase and its enzyme class number is E.C. 3.1.1.3 <ref name="1HPL PDB SUM">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1hpl&template=main.html] 1HPL PDB SUM </ref>.  The reaction catalyzed by this enzyme is shown below.  [[Image:Picture 1.png]]
-Pancreatic lipase specifically catalyzes the hydrolysis of triacylglycerols into 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>.  Pancreatic liapase is a 50 kDa protein, consisting of two identical, 449 residue chains <ref name= "1HPL PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL] 1HPL PDB</ref>.  The determination of the structure and function of lipase was a gradual process.  Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846.  It wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>.  In recent years, determination of the crystal structure of pancreatic lipase has become the focus and many scientists have worked to further this.
+Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>.  Pancreatic liapase is a 50 kDa protein, consisting of two identical, 449 residue chains <ref name= "1HPL PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=1HPL] 1HPL PDB</ref>.  The determination of the structure and function of lipase was a gradual process.  Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846.  It wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>.  In recent years, determination of the crystal structure of pancreatic lipase has become the focus and many scientists have worked to further this.
 <applet load='1HPL' size='400' frame='true' align='right' scene='Sandbox_45/Pancreatic_lipase/1' caption='Horse Pancreatic Lipase at 2.3 Angstroms Resolution (PDB ID:  1HPL)'  />