Lipase
In
Structure and catalytic mechanism
Classically, lipases catalyse the hydrolysis of triglycerides:
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Lipases are
A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of
Physiological distribution
Lipases are involved in diverse biological processes which range from routine metabolism of
- In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
- Other lipase enzymes, such as extracellularspaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body.
- Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host).
- Certain wasp and bee venoms contain phospholipases that enhance the effects of injury and inflammation delivered by a sting.
- As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology.
- sebum into oleic acid and increase skin cell production, causing dandruff.[14]
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]
Human lipases
| 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 |
||
| lysosomal lipase | LIPA | interior space of organelle: lysosome | Also referred to as lysosomal acid lipase (LAL or LIPA) or acid cholesteryl ester hydrolase | Wolman disease are both caused by mutations in the gene encoding lysosomal lipase.[19]
|
| hepatic lipase | LIPC | endothelium | Hepatic lipase acts on the remaining low density lipoprotein ). |
– |
| lipoprotein lipase | LPL or "LIPD" | endothelium | 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.
Uses
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].
Biomedicine
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
See also
- Alpha toxin
- Pathology
- Lysosomal acid lipase deficiency
- Peripheral membrane proteins
- Phospholipase A
- Phospholipase C
- Triglyceride lipase
- Phospholipase A2
- Outer membrane phospholipase A1
- Patatin-like phospholipase
References
- ^ PMID 11514232.
- PMID 12895591.
- PMID 12401200.
- ^ S2CID 18615547.
- ^ S2CID 37423900.
- S2CID 37423900.
- PMID 9379946.
- PMID 9379930.
- PMID 8939760.
- S2CID 4308111.
- PMID 1512245.
- PMID 8791422.
- PMID 7592717.
- ^ Genetic Code of Dandruff Cracked – BBC News
- PMID 9847359.
- PMID 11961250.
- S2CID 2231039.
- PMID 12454260.
- ^ Omim – Wolman Disease
- ^ Familial lipoprotein lipase deficiency – Genetics Home Reference
- PMID 11334614.
- PMID 9605548.
- PMID 9748646.
- S2CID 206934353.
- PMID 11356369.
- .
- PMID 15999195.
- .
- .
- doi:10.15227/orgsyn.073.0036.)
{{cite journal}}: CS1 maint: multiple names: authors list (link - .
- ^ "Lipase – TheTest". Lab Tests Online. Retrieved 12 May 2014.
- ^ "Anthera Pharmaceuticals – Sollpura." Anthera Pharmaceuticals – Sollpura. N.p., n.d. Web. 21 July 2015. <http://www.anthera.com/pipeline/science/sollpura.html Archived 2015-07-18 at the Wayback Machine>.
- S2CID 23597738.
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), 2003
External links
- Lipase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
