Lipase: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 18: | Line 18: | ||
==Lipase Catalytic Mechanism== | ==Lipase Catalytic Mechanism== | ||
==Hydrophobicity/Hydrophillicity== | |||
The <scene name='Lipase/Hydrophobic_space_fill/1'>space fill model</scene> is a useful representation of the distribution of hydrophobic and hydrophillic residues. Hydrophobic residues are shown in red and hydrophillic residues in blue. When the hydrophillic residues are removed and only <scene name='Lipase/Hydrophobic_space_fill/2'>hydrophobic residues</scene> are shown, it is clear that the core of the enzyme is made of hydrophobic residues while the hydrophillic residues are mainly located on the surface of the enzyme. | |||
Although a diverse array of lipase enzymes are found in nature, occupying diverse protein scaffolds, most are built upon an alpha/beta hydrolase fold<ref>PMID: 1678899</ref><ref>PMID:1409539 </ref> and possess a [[chymotrypsin]]-like <scene name='Lipase/Catalytic_site_outerview/1'>catalytic triad </scene>comprised of an acidic residue, a histidine, and a serine nucleophile. In the case of the images above of a horse pancreatic lipase, the catalytic triad is comprised of <scene name='Lipase/Catalytic_triad/4'>Ser 152, Asp 176 and His 263. </scene><ref>PMID:8182745</ref> | Although a diverse array of lipase enzymes are found in nature, occupying diverse protein scaffolds, most are built upon an alpha/beta hydrolase fold<ref>PMID: 1678899</ref><ref>PMID:1409539 </ref> and possess a [[chymotrypsin]]-like <scene name='Lipase/Catalytic_site_outerview/1'>catalytic triad </scene>comprised of an acidic residue, a histidine, and a serine nucleophile. In the case of the images above of a horse pancreatic lipase, the catalytic triad is comprised of <scene name='Lipase/Catalytic_triad/4'>Ser 152, Asp 176 and His 263. </scene><ref>PMID:8182745</ref> | ||
