Lipase

In biochemistry, lipase (/ˈlaɪpeɪs, ˈlaɪpeɪz/ LY-payss, LY-payz) refers to a class of enzymes that catalyzes the hydrolysis of fats.

[4] Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms.

For example, human pancreatic lipase (HPL),[5] converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.

A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of protein folds and catalytic mechanisms.

[10][11] Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling[12] and inflammation.

[17] Other lipases include LIPH, LIPI, LIPJ, LIPK, LIPM, LIPN, MGLL, DAGLA, DAGLB, and CEL.

[4] Lipases are catalysts for hydrolysis of esters and are useful outside of the cell, a testament to their wide substrate scope and ruggedness.

The ester hydrolysis activity of lipases has been well evaluated for the conversion of triglycerides into biofuels or their precursors.

[citation needed] Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas.

[citation needed] Lipase assist in the breakdown of fats in those undergoing pancreatic enzyme replacement therapy (PERT).

A computer-generated image of a type of pancreatic lipase (PLRP2) from the guinea pig. PDB : 1GPL ​.