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Class of enzymes which cleave fats via hydrolysis From Wikipedia, the free encyclopedia
In biochemistry, lipase (/ˈlaɪpeɪs, ˈlaɪpeɪz/ LY-payss, LY-payz) refers to a class of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol, phospholipids, and of lipid-soluble vitamins[1][2] and sphingomyelinases;[3] however, these are usually treated separately from "conventional" lipases. Unlike esterases, which function in water, lipases "are activated only when adsorbed to an oil–water interface".[4] Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms.
Classically, lipases catalyse the hydrolysis of triglycerides:
Lipases are serine hydrolases, i.e. they function by transesterification generating an acyl serine intermediate. Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3). 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. However, most are built on an alpha/beta hydrolase fold[6][7][8][9] and employ a chymotrypsin-like hydrolysis mechanism using a catalytic triad consisting of a serine nucleophile, a histidine base, and an acid residue, usually aspartic acid.[10][11]
Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling[12] and inflammation.[13] Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces.
Genes encoding lipases are even present in certain viruses.[15][16]
Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.[17]
| Name | Gene | Location | Description | Disorder |
|---|---|---|---|---|
| bile salt-dependent lipase | BSDL | pancreas, breast milk | aids in the digestion of fats[1] | |
| pancreatic lipase | PNLIP | digestive juice | Human pancreatic lipase (HPL) is the main enzyme that breaks down dietary fats in the human digestive system.[5] To exhibit optimal enzyme activity in the gut lumen, PL requires another protein, colipase, which is also secreted by the pancreas.[18] | |
| lysosomal lipase | LIPA | interior space of organelle: lysosome | Also referred to as lysosomal acid lipase (LAL or LIPA) or acid cholesteryl ester hydrolase | Cholesteryl ester storage disease (CESD) and Wolman disease are both caused by mutations in the gene encoding lysosomal lipase.[19] |
| hepatic lipase | LIPC | endothelium | Hepatic lipase acts on the remaining lipids carried on lipoproteins in the blood to regenerate LDL (low density lipoprotein). | – |
| lipoprotein lipase | LPL or "LIPD" | endothelium | Lipoprotein lipase functions in the blood to act on triacylglycerides carried on VLDL (very low density lipoprotein) so that cells can take up the freed fatty acids. | Lipoprotein lipase deficiency is caused by mutations in the gene encoding lipoprotein lipase.[20][21] |
| hormone-sensitive lipase | LIPE | intracellular | – | – |
| gastric lipase | LIPF | digestive juice | Functions in the infant at a near-neutral pH to aid in the digestion of lipids | – |
| endothelial lipase | LIPG | endothelium | – | – |
| pancreatic lipase related protein 2 | PNLIPRP2 or "PLRP2" – | digestive juice | – | – |
| pancreatic lipase related protein 1 | PNLIPRP1 or "PLRP1" | digestive juice | Pancreatic lipase related protein 1 is very similar to PLRP2 and PL by amino acid sequence (all three genes probably arose via gene duplication of a single ancestral pancreatic lipase gene). However, PLRP1 is devoid of detectable lipase activity and its function remains unknown, even though it is conserved in other mammals.[22][23] | - |
| lingual lipase | ? | saliva | Active at gastric pH levels. Optimum pH is about 3.5-6. Secreted by several of the salivary glands (Ebner's glands at the back of the tongue (lingua), the sublingual glands, and the parotid glands) | – |
Other lipases include LIPH, LIPI, LIPJ, LIPK, LIPM, LIPN, MGLL, DAGLA, DAGLB, and CEL.
In the commercial sphere, lipases are widely used in laundry detergents. Several thousand tons per year are produced for this role.[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.[24][25][26][27]
Lipases are chiral, which means that they can be used for the enantioselective hydrolysis prochiral diesters.[28] Several procedures have been reported for applications in the synthesis of fine chemicals.[29][30][31]
Lipases are generally animal sourced, but can also be sourced microbially.[citation needed]
Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas.[32] Measured serum lipase values may vary depending on the method of analysis.[citation needed]
Lipase assist in the breakdown of fats in those undergoing pancreatic enzyme replacement therapy (PERT). It is a component in Sollpura (Liprotamase).[33][34]
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