Pancreatic lipase family
Complex of human pancreatic lipase with colipase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Lipase | ||||||||
| Pfam | PF00151 | ||||||||
| InterPro | IPR013818 | ||||||||
| PROSITE | PDOC00110 | ||||||||
| SCOP2 | 1lpa / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 127 | ||||||||
| OPM protein | 1lpa | ||||||||
| |||||||||
Pancreatic lipases (EC 3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes.
At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC 3.1.1.34), 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 (EC 2.3.1.43) (LCAT), which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.