Pancreatic lipase (IPR002331)

Short name: Lipase_panc

Overlapping homologous superfamilies

Family relationships


Triglyceride lipases (EC: are lipolytic enzymes that hydrolyse ester linkages of triglycerides [PMID: 3147715]. 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:, which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [PMID: 2917565]. Pancreatic lipase (triacylglycerol acylhydrolase, EC: plays a key role in dietary fat absorption by hydrolysing dietary long chain triacyl-glycerol to free fatty acids and monoacylglycerols in the intestinal lumen [PMID: 2479644]. The activity of lipase is stimulated by colipase in the presence of bile acids.

The 3D structure of human pancreatic lipase has been determined by X-ray crystallography [PMID: 2106079]. The enzyme is a single-chain glycoprotein of 449 amino acids. Structural results suggest that Ser 152 is the nucleophilic residue essential for catalysis [PMID: 2106079]. The residue is located in the N-terminal domain at the C-terminal edge of a doubly-wound parallel beta-sheet, and forms part of an Asp-His-Ser triad that is chemically analogous to, but structurally different from, that of the serine proteases [PMID: 2106079]. The putative hydrolytic site is covered by a surface loop, and is thus inaccessible to solvent. It is thought that interfacial activation may involve a reorientation of this flap, not only in pancreatic lipases but also in the related hepatic and lipoprotein lipases [PMID: 2106079].

GO terms

Biological Process

GO:0006629 lipid metabolic process

Molecular Function

GO:0004806 triglyceride lipase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.