Product Code Database
Pancreatic lipases () are a protein family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes.
At least three tissue-specific exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL).
Pancreatic lipase contains two protein domains. The one toward the N terminus is an α/β hydrolase, whereas the one toward the C terminus plays a role in binding to colipase, a protein needed in order for the lipase to become activated.
The most conserved region in all these proteins is centred on a serine residue which has been shown to participate, with a histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase () (LCAT), which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.
Bile salts secreted from the liver and stored in gallbladder are released into the duodenum, where they coat and Emulsion large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal.
Unlike some pancreatic enzymes that are activated by proteolytic cleavage (e.g., trypsinogen), pancreatic lipase is secreted in its final form. However, it becomes efficient only in the presence of colipase in the duodenum.
In humans, pancreatic lipase is encoded by the PNLIP gene.
One peptide selected by phage display was found to inhibit pancreatic lipase.
|
|
