Lipase: Difference between revisions
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This catalytic triad functions like most found in nature, first with the Aspartic acid forming a hydrogen bond with His 263, increasing the pKa of the histidine imidazole nitrogen. This allows the Histidine to act as a powerful general base and deprotonate the serine. The deprotonated serine then can serve as a nucleophile and attack the glycerol backbone of the lipid substrate. A water molecule then donates a proton to the histidine, creating a reactive hydroxyl anion, which can attack the carbonyl carbon of the lipid, releasing the catalytic serine and creating monoglyceride and fatty acid monomers that diffuse away. | This catalytic triad functions like most found in nature, first with the Aspartic acid forming a hydrogen bond with His 263, increasing the pKa of the histidine imidazole nitrogen. This allows the Histidine to act as a powerful general base and deprotonate the serine. The deprotonated serine then can serve as a nucleophile and attack the glycerol backbone of the lipid substrate. A water molecule then donates a proton to the histidine, creating a reactive hydroxyl anion, which can attack the carbonyl carbon of the lipid, releasing the catalytic serine and creating monoglyceride and fatty acid monomers that diffuse away. | ||
<scene name='Lipase/Catalytic_triad/ | <scene name='Lipase/Catalytic_triad/6'>catalytic triad</scene> | ||
<scene name='Lipase/Catalytic_triad_with_oxyanion/ | <scene name='Lipase/Catalytic_triad_with_oxyanion/2'>oxyanion hole</scene> | ||
==Inhibition of Pancreatic Lipase== | ==Inhibition of Pancreatic Lipase== | ||
