Protein Domain : Pancreatic lipase IPR002331

Type	Family
Description	Triglyceride lipases ( ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides []. Lipases are widely distributed inanimals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates: pancreatic, hepatic and gastric/lingual. Theselipases are closely related to each other and to lipoprotein lipase (), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [].Pancreatic lipase (triacylglycerol acylhydrolase, ) 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[ ]. The activity of lipase is stimulated by colipase in the presence ofbile acids. The 3D structure of human pancreatic lipase has been determined by X-ray crystallography []. The enzyme is a single-chain glycoprotein of 449 amino acids. Structural results suggest that Ser 152 is the nucleophilic residue essential for catalysis []. The residue is located in the N-terminal domainat the C-terminal edge of a doubly-wound parallel β-sheet, and forms part of an Asp-His-Ser triad that is chemically analogous to, but structurallydifferent from, that of the serine proteases [ ]. The putative hydrolyticsite is covered by a surface loop, and is thus inaccessible to solvent. It is thought that interfacial activation may involve a reorientation ofthis flap, not only in pancreatic lipases but also in the related hepatic and lipoprotein lipases [].
Short Name	Lipase_panc