Lipase: Difference between revisions
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== '''Protein - Substrate Interactions''' == | == '''Protein - Substrate Interactions''' == | ||
Lipase binds <scene name='Lipase/Substrate_contacts/1'>substrates such as cholesteryl linoleate</scene> with numerous hydrophobic contacts. As is seen here the lipase interacts with the alkyl group of cholesteryl linoleate via a hydrophobic rift within the protein. This rift orients the molecule to optimize the lipolysis reaction. | Lipase binds <scene name='Lipase/Substrate_contacts/1'>substrates such as cholesteryl linoleate</scene> with numerous hydrophobic contacts. As is seen here the lipase interacts with the alkyl group of cholesteryl linoleate via a hydrophobic rift within the protein. This rift orients the molecule to optimize the lipolysis reaction. | ||
Shown in this scene is lipase from ''Candida rugosa'' in <scene name='Lipase/Complex_2/1'>complex</scene> with two molecules of cholesteryl linoleate (grey). The active site residues including SER152, ASP176, and HIS263 are shown in red stick representation. Lipase can accommodate two molecules of cholesteryl linoleate, or whatever its substrate maybe, due to the fact that it's two identical subunits catalyze an identical reaction. | Shown in this scene is lipase from the yeast ''Candida rugosa'' in <scene name='Lipase/Complex_2/1'>complex</scene> with two molecules of cholesteryl linoleate (grey). The active site residues including SER152, ASP176, and HIS263 are shown in red stick representation. Lipase can accommodate two molecules of cholesteryl linoleate, or whatever its substrate maybe, due to the fact that it's two identical subunits catalyze an identical reaction. One lipase molecule can catalyze two lipolysis reactions at a time. | ||
