Lipase

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

A lipase (/ˈlps/, /ˈlɪps/, /-pz/) is any enzyme that catalyzes the hydrolysis of fats (lipids).[1] Lipases are a subclass of the esterases.

Lipases perform essential roles in the digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. Genes encoding lipases are even present in certain viruses.[2][3]

Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3)(small intestine). For example, human pancreatic lipase (HPL),[4] which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.

Several other types of lipase activities exist in nature, such as phospholipases [5] and sphingomyelinases,[6] however these are usually treated separately from "conventional" lipases.

Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, Candida albicans has a large number of different lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.[7]

Structure and catalytic mechanism

Although a diverse array of genetically distinct lipase enzymes are found in nature; and, they represent several types of protein folds and catalytic mechanisms, most of them are built on an alpha/beta hydrolase fold[8][9][10][11] 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).[12][13]

Physiological distribution

Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling[14] and inflammation.[15] Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces.

Human lipases

The main lipases of the human digestive system are pancreatic lipase (PL) and pancreatic lipase related protein 2 (PLRP2), which are secreted by the pancreas. Humans also have several other related enzymes, including hepatic lipase, endothelial lipase, and lipoprotein lipase. Not all of these lipases function in the gut (see table).

Name Gene Location Description Disorder
bile salt-dependent lipase bsdl pancreas, breast milk aids in the digestion of fats
pancreatic lipase PNLIP digestive juice In order to exhibit optimal enzyme activity in the gut lumen, PL requires another protein, colipase, which is also secreted by the pancreas.[17]
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.[18]
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.[19][20]
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.[21][22] -
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.

There also are a diverse array of phospholipases, but these are not always classified with the other lipases.

Industrial uses

Lipases serve important roles in human practices as ancient as yogurt and cheese fermentation. However, lipases are also being exploited as cheap and versatile catalysts to degrade lipids in more modern applications. For instance, a biotechnology company has brought recombinant lipase enzymes to market for use in applications such as baking, laundry detergents and even as biocatalysts[23] in alternative energy strategies to convert vegetable oil into fuel.[24][25] High enzyme activity lipase can replace traditional catalyst in processing biodiesel, as this enzyme replaces chemicals in a process which is otherwise highly energy intensive,[26] and can be more environmentally friendly and safe. Industrial application of lipases requires process intensification for continuous processing using tools like continuous flow microreactors at small scale.[27][28] Lipases are generally animal sourced, but can also be sourced microbially.

Diagnostic use

Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas.[29] Measured serum lipase values may vary depending on the method of analysis.

Medical use

Lipase can also assist in the breakdown of fats into lipids in those undergoing pancreatic enzyme replacement therapy(PERT). It is a key component in Sollpura (Liprotamase).[30]

Additional images

See also

References

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  3. Girod A, Wobus C, Zádori Z, Ried M, Leike K, Tijssen P, Kleinschmidt J, Hallek M (2002). "The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity". J Gen Virol 83 (Pt 5): 973–8. PMID 11961250.
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  7. Hube B, Stehr F, Bossenz M, Mazur A, Kretschmar M, Schafer W (2000). "Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members". Arch. Microbiol. 174 (5): 362–374. doi:10.1007/s002030000218. PMID 11131027.
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  13. Lowe ME (1992). "The catalytic site residues and interfacial binding of human pancreatic lipase". J Biol Chem 267 (24): 17069–73. PMID 1512245.
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  16. Genetic Code of Dandruff Cracked - BBC News
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  18. Omim - Wolman Disease
  19. Familial lipoprotein lipase deficiency - Genetics Home Reference
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  21. Crenon I, Foglizzo E, Kerfelec B, Verine A, Pignol D, Hermoso J, Bonicel J, Chapus C (1998). "Pancreatic lipase-related protein type I: a specialized lipase or an inactive enzyme". Protein Eng 11 (2): 135–42. doi:10.1093/protein/11.2.135. PMID 9605548.
  22. De Caro J, Carriere F, Barboni P, Giller T, Verger R, De Caro A (1998). "Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species". Biochim Biophys Acta 1387 (1–2): 331–41. doi:10.1016/S0167-4838(98)00143-5. PMID 9748646.
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  25. Ban K, Kaieda M, Matsumoto T, Kondo A, Fukuda H (2001). "Whole cell biocatalyst for biodiesel fuel production utilizing Rhizopus oryzae cells immobilized within biomass support particles". Biochem Eng J 8 (1): 39–43. doi:10.1016/S1369-703X(00)00133-9. PMID 11356369.
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  27. Bhangale, Atul. "Enzyme-Catalyzed Polymerization of End-Functionalized Polymers in a Microreactor". Macromolecules 45: 7000–7008. doi:10.1021/ma301178k.
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  30. "Anthera Pharmaceuticals - Sollpura." Anthera Pharmaceuticals - Sollpura. N.p., n.d. Web. 21 July 2015. <http://www.anthera.com/pipeline/science/sollpura.html>.

25. Gulzar, Bio-degradation of hydrocarbons using different bacterial and fungal species. Published in international conference on biotechnology and neurosciences. CUSAT (cochin university of science and technology), 2004

External links

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