Lipase: Difference between revisions

Eric Martz (talk | contribs)
No edit summary
Eric Martz (talk | contribs)
No edit summary
Line 36: Line 36:
A water molecule then donates a proton to the histidine, creating a reactive hydroxyl anion. The hydroxyl anion can then attack the carbonyl carbon of the lipid, forming another negatively charged tetrahedral intermediate which is stabilized in the oxyanion hole (Reaction 3).   
A water molecule then donates a proton to the histidine, creating a reactive hydroxyl anion. The hydroxyl anion can then attack the carbonyl carbon of the lipid, forming another negatively charged tetrahedral intermediate which is stabilized in the oxyanion hole (Reaction 3).   


[[Image:M0218.stg03.gif|center|]]
[[Image:M0218.stg03r.gif|center|]]
Upon reformation of the carbonyl, the catalytic serine is released and monoglyceride and fatty acid monomers diffuse away (Reaction 4).   
Upon reformation of the carbonyl, the catalytic serine is released and monoglyceride and fatty acid monomers diffuse away (Reaction 4).   


[[Image:M0218.stg04.gif|center|]]
[[Image:M0218.stg04r.gif|center|]]


== '''Inhibition of Pancreatic Lipase''' ==
== '''Inhibition of Pancreatic Lipase''' ==

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