Lipase: Difference between revisions

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*  The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />
*  The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />
*  The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters.  For details see [[Hormone sensitive lipase]].<br />
*  The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters.  For details see [[Hormone sensitive lipase]].<br />
*  '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol.  MAGL functions together with LIPE.  For details see [[Monoglyceride lipase]].br/>
*  '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol.  MAGL functions together with LIPE.  For details see [[Monoglyceride lipase]].


The reaction catalyzed by the enzyme is shown below.  
The reaction catalyzed by the enzyme is shown below.  
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[[Image:Picture 1.png]]   
[[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>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. 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.  However, 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 primary focus as many scientists have worked to further this.<br />
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>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. 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.  However, 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 primary focus as many scientists have worked to further this.<br />
=='''See also'''==<br />
 
==See also==
* [[Molecular Playground/Pancreatic Lipase]]<br />
* [[Molecular Playground/Pancreatic Lipase]]<br />
* [[Lipase lid morph]]<br />
* [[Lipase lid morph]]<br />
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* [[Monoglyceride lipase]]<br />
* [[Monoglyceride lipase]]<br />
* [[Human gastric lipase]]<br />
* [[Human gastric lipase]]<br />
* [[Lipoprotein Lipase (LPL) complexed with GPIHBP1]]<br />
* [[Lipase (Hebrew)]]<br />
* [[Lipase (Hebrew)]]<br />
* [[Lipid metabolism]]


== '''Structure''' ==
== '''Structure''' ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

David Canner, Joel L. Sussman, Eran Hodis, Alexander Berchansky, Michal Harel, Stephanie Schell, Natalie Ziegler, Quinn R. Murray, Katelyn Clark, Leben Tadesse, Eric Martz