Lipase: Difference between revisions

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'''Lipase''' is a subclass of esterases which catalyzes the hydrolysis of ester bonds in lipid substrates and is essential for fat digestion. It is primarily produced in the pancreas, but can be found in the mouth and stomach as well. The <scene name='Lipase/Lipase_starting_scene/2'>lipase</scene> typically digests fat lipids into monoglycerides and free fatty acids, with the resulting monomers subsequently shuttled to the small intestine and eventually absorbed into the lymphatic system. See also [[Molecular Playground/Pancreatic Lipase]].

==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 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]]

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: @@
 '''Lipase''' is a subclass of esterases which catalyzes the hydrolysis of ester bonds in lipid substrates and is essential for fat digestion. It is primarily produced in the pancreas, but can be found in the mouth and stomach as well. The <scene name='Lipase/Lipase_starting_scene/2'>lipase</scene> typically digests fat lipids into monoglycerides and free fatty acids, with the resulting monomers subsequently shuttled to the small intestine and eventually absorbed into the lymphatic system.  See also [[Molecular Playground/Pancreatic Lipase]].
+==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 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]]
+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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