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[[File:Lipase PLRP2.png|right|thumb|300px|A computer-generated image of a type of pancreatic lipase (PLRP2) from the guinea pig. {{PDB|1GPL}}.]]

A '''lipase''' ({{IPAc-en|ˈ|l|aɪ|p|eɪ|s}}, {{IPAc-en|-|p|eɪ|z}}) is any [[enzyme]] that [[catalyze]]s the [[hydrolysis]] of [[fat]]s ([[lipid]]s).<ref>{{cite journal |author=Svendsen A |title=Lipase protein engineering |journal=Biochim Biophys Acta |volume=1543 |issue=2 |pages=223–228 |year=2000 |pmid=11150608 |doi=10.1016/S0167-4838(00)00239-9}}</ref> Lipases are a subclass of the [[esterase]]s.

Lipases perform essential roles in [[digestion]], transport and processing of dietary lipids (e.g. [[triglycerides]], [[fat]]s, [[oil]]s) in most, if not all, living [[organism]]s. [[Genes]] encoding lipases are even present in certain [[virus]]es.<ref>{{cite journal |vauthors=Afonso C, Tulman E, Lu Z, Oma E, Kutish G, Rock D |title=The Genome of Melanoplus sanguinipes Entomologists |journal=J Virol |volume=73 |issue=1 |pages=533–52 |year=1999 |pmid=9847359 |pmc=103860}}</ref><ref>{{cite journal |vauthors=Girod A, Wobus C, Zádori Z, Ried M, Leike K, Tijssen P, Kleinschmidt J, Hallek M |title=The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity |journal=J Gen Virol |volume=83 |issue=Pt 5 |pages=973–8 |year=2002 |pmid=11961250 |doi=10.1099/0022-1317-83-5-973}}</ref>

Most lipases act at a specific position on the [[glycerol]] backbone of a lipid [[substrate (chemistry)|substrate]] (A1, A2 or A3)(small intestine). For example, [[human pancreatic lipase]] (HPL),<ref>{{cite journal |author1=Winkler FK |author2=D'Arcy A |author3=W Hunziker |title=Structure of human pancreatic lipase |journal=Nature|volume=343 |issue=6260 |pages=771–774 |year= 1990 |pmid=2106079 |doi=10.1038/343771a0}}</ref> which is the main enzyme that breaks down dietary [[fat]]s in the [[human]] [[digestive system]], converts [[triglyceride]] substrates found in ingested oils to [[monoglyceride]]s and two [[fatty acid]]s.

Several other types of lipase activities exist in nature, such as [[phospholipase]]s <ref>{{cite journal |author1=Diaz, B.L. |author2=J. P. Arm. |title=Phospholipase A(2) |journal=Prostaglandins Leukot Essent Fatty Acids |volume= 69|pages=87–97|year=2003 |pmid=12895591 |doi=10.1016/S0952-3278(03)00069-3 |issue=2–3}}</ref> and [[sphingomyelinase]]s;<ref>{{cite journal |vauthors=Goñi F, Alonso A |title=Sphingomyelinases: enzymology and membrane activity |journal=FEBS Lett |volume=531 |issue=1 |pages=38–46 |year=2002 |pmid=12401200 |doi=10.1016/S0014-5793(02)03482-8}}</ref> 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-[[lipolysis|lipolytic]] activity, which may contribute to the persistence and virulence of ''C. albicans ''in human tissue.<ref>{{cite journal |vauthors=Hube B, Stehr F, Bossenz M, Mazur A, Kretschmar M, Schafer W |title=Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members |journal=Arch. Microbiol. |volume=174 |issue=5 |pages=362–374 |year=2000 |pmid=11131027 |doi=10.1007/s002030000218}}</ref>

==Structure and catalytic mechanism==
Although a diverse array of [[genetics|genetic]]ally distinct lipase enzymes are found in nature; and, they represent several types of [[protein folding|protein folds]] and catalytic mechanisms, most of them are built on an [[alpha/beta hydrolase fold]]<ref name="Winkler FK, D'Arcy A, and W Hunziker 1990 771–774">{{cite journal |author1=Winkler FK |author2=D'Arcy A |author3=W Hunziker |title=Structure of human boob pancreatic lipase |journal=Nature|volume=343 |issue=6260 |pages=771–774 |year= 1990 |pmid=2106079 |doi=10.1038/343771a0}}</ref><ref>{{cite journal |vauthors=Schrag J, Cygler M |title=Lipases and [[alpha/beta hydrolase fold]] |journal=Methods Enzymol |volume=284 |issue= |pages=85–107 |year= 1997|pmid=9379946 |doi=10.1016/S0076-6879(97)84006-2 |series=Methods in Enzymology |isbn=978-0-12-182185-2}}</ref><ref>{{cite journal |author1=Egmond, M. R. |author2=C. J. van Bemmel |title=Impact of Structural Information on Understanding of Lipolytic Function |journal=Methods Enzymol |volume=284 |pages=119–129 |year= 1997 |pmid=9379930 |doi=10.1016/S0076-6879(97)84008-6 |series=Methods in Enzymology |isbn=978-0-12-182185-2}}</ref><ref>{{cite journal |author1=Withers-Martinez C |author2=Carriere F |author3=Verger R |author4=Bourgeois D |author5=C Cambillau |title=A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig|journal=Structure|volume=4|issue=11 |pages= 1363–74 |year=1996 |pmid=8939760|doi=10.1016/S0969-2126(96)00143-8}}</ref> 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]]).<ref>{{cite journal |author=Brady, L. |author2=A. M. Brzozowski |author3=Z. S. Derewenda |author4=E. Dodson |author5=G. Dodson |author6=S. Tolley |author7=J. P. Turkenburg |author8=L. Christiansen |author9=B. Huge-Jensen |author10=L. Norskov |title=A serine protease triad forms the catalytic centre of a triacylglycerol lipase |journal=Nature |volume=343 |issue=6260 |pages=767–70 |year=1990 |pmid=2304552 |doi=10.1038/343767a0|display-authors=etal}}</ref><ref>{{cite journal |author=Lowe ME |title=The catalytic site residues and interfacial binding of human pancreatic lipase |journal=J Biol Chem |volume=267 |issue=24 |pages=17069–73 |year=1992 |pmid=1512245}}</ref>

==Physiological distribution==

Lipases are involved in diverse biological processes which range from routine metabolism of [[Diet (nutrition)|dietary]] [[triglycerides]] to [[cell signaling]]<ref>{{cite journal |author1=Spiegel S |author2=Foster D |author3=R Kolesnick |title=Signal transduction through lipid second messengers|journal=Current Opinion in Cell Biology|volume=8|issue=2 |pages=159–67 |year=1996 |pmid=8791422 |doi=10.1016/S0955-0674(96)80061-5}}</ref> and [[inflammation]].<ref>{{cite journal |author1=Tjoelker LW |author2=Eberhardt C |author3=Unger J |author4=Trong HL |author5=Zimmerman GA |author6=McIntyre TM |author7=Stafforini DM |author8=Prescott SM |author9=PW Gray |title=Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad |journal=J Biol Chem |volume=270 |issue=43 |pages=25481–7 |year=1995 |pmid=7592717 |doi=10.1074/jbc.270.43.25481}}</ref> Thus, some lipase activities are confined to specific compartments within [[cell (biology)|cell]]s while others work in extracellular spaces.

* In the example of [[lysosomal lipase]], the enzyme is confined within an [[organelle]] called the [[lysosome]].
* Other lipase enzymes, such as [[Human pancreatic lipase|pancreatic lipases]], are secreted into [[extracellular]] spaces 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 [[phospholipase]]s that enhance the effects of injury and inflammation delivered by a sting.
* As [[biological membrane]]s are integral to living cells and are largely composed of [[phospholipid]]s, lipases play important roles in [[cell biology]].
*''[[Malassezia globosa]]'', a fungus that is thought to be the cause of human [[dandruff]], uses lipase to break down [[sebum]] into [[oleic acid]] and increase skin cell production, causing dandruff.<ref>[http://news.bbc.co.uk/2/hi/health/7080434.stm Genetic Code of Dandruff Cracked - BBC News]</ref>

==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).

{| class="wikitable"
| '''Name''' || '''Gene''' || '''Location''' || '''Description''' || '''Disorder'''
|-
| [[bile salt dependent lipase|bile salt-dependent lipase]] || bsdl || [[pancreas]], [[breast milk]] || aids in the digestion of fats ||
|-
| [[pancreatic lipase]] || {{Gene|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.<ref>{{cite journal |author=Lowe ME |title=The triglyceride lipases of the pancreas |journal= J Lipid Res |volume=43 |issue=12 |pages=2007–16 |year=2002 |pmid=12454260 |doi=10.1194/jlr.R200012-JLR200}}</ref> ||
|-
| [[lysosomal lipase]] || {{Gene|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.<ref>[https://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=278000 Omim - Wolman Disease<!-- Bot generated title -->]</ref>
|-
| [[hepatic lipase]] || {{Gene|LIPC}} || [[endothelium]] || Hepatic lipase acts on the remaining [[lipid]]s carried on lipoproteins in the blood to regenerate LDL ([[low density lipoprotein]]). || -
|-
| [[lipoprotein lipase]] || {{Gene|LPL}} or "LIPD" || [[endothelium]] || [[Lipoprotein lipase]] functions in the [[blood]] to act on [[triacylglyceride]]s carried on [[Very low-density lipoprotein|VLDL]] (very low density [[lipoprotein]]) so that cells can take up the freed [[fatty acid]]s. || [[Lipoprotein lipase deficiency]] is caused by [[mutation]]s in the [[gene]] encoding [[lipoprotein lipase]].<ref>[http://ghr.nlm.nih.gov/condition=lipoproteinlipasedeficiencyfamilial Familial lipoprotein lipase deficiency - Genetics Home Reference<!-- Bot generated title -->]</ref><ref>{{cite journal |vauthors=Gilbert B, Rouis M, Griglio S, de Lumley L, Laplaud P |title=Lipoprotein lipase (LPL) deficiency: a new patient homozygote for the preponderant mutation Gly188Glu in the human LPL gene and review of reported mutations: 75 % are clustered in exons 5 and 6 |journal=Ann Genet |volume=44 |issue=1 |pages=25–32 |year= 2001|pmid=11334614 |doi=10.1016/S0003-3995(01)01037-1}}</ref>
|-
| [[hormone-sensitive lipase]] || {{Gene|LIPE}} || [[intracellular]] || - || -
|-
| [[gastric lipase]] || {{Gene|LIPF}} || [[digestive juice]] || Functions in the infant at a near-neutral pH to aid in the digestion of lipids || -
|-
| [[endothelial lipase]] || {{Gene|LIPG}} || [[endothelium]] || - || -
|-
| [[pancreatic lipase related protein 2]] || {{Gene|PNLIPRP2}} or "PLRP2" - || [[digestive juice]]|| - || -
|-
| [[pancreatic lipase related protein 1]] || {{Gene|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 [[mammal]]s.<ref>{{cite journal |vauthors=Crenon I, Foglizzo E, Kerfelec B, Verine A, Pignol D, Hermoso J, Bonicel J, Chapus C |title=Pancreatic lipase-related protein type I: a specialized lipase or an inactive enzyme|journal=Protein Eng|volume=11|issue=2 |pages= 135–42 |year=1998 |pmid=9605548 |doi=10.1093/protein/11.2.135}}</ref><ref>{{cite journal |vauthors=De Caro J, Carriere F, Barboni P, Giller T, Verger R, De Caro A |title=Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species|journal=Biochim Biophys Acta|volume=1387|issue=1–2 |pages= 331–41 |year=1998 |pmid=9748646 |doi=10.1016/S0167-4838(98)00143-5}}</ref> || -
|-
| [[lingual lipase]] || ? || [[saliva]] || Active at gastric pH levels. Optimum pH is about 3.5-6. Secreted by several of the [[salivary gland]]s ([[Von Ebner's gland|Ebner's gland]]s at the back of the [[tongue]] (lingua), the [[sublingual gland]]s, and the [[parotid gland]]s) || -
|}

Other lipases include {{Gene|LIPH}}, {{Gene|LIPI}}, {{Gene|LIPJ}}, {{Gene|LIPK}}, {{Gene|LIPM}}, {{Gene|LIPN}}, {{Gene|MGLL}}, {{Gene|DAGLA}}, {{Gene|DAGLB}}, and {{Gene|CEL}}.

There also are a diverse array of [[phospholipase]]s, 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 [[biocatalyst]]s<ref>{{cite journal |vauthors=Guo Z, Xu X |title=New opportunity for enzymatic modification of fats and oils with industrial potentials|journal=Org Biomol Chem|volume=3|issue=14 |pages=2615–9 |year=2005 |pmid=15999195 |doi=10.1039/b506763d}}</ref> in [[alternative energy]] strategies to convert vegetable oil into fuel.<ref>{{cite journal |vauthors=Gupta R, Gupta N, Rathi P |title=Bacterial lipases: an overview of production, purification and biochemical properties|journal=Appl Microbiol Biotechnol|volume=64|issue=6 |pages=763–81 |year=2004 |pmid=14966663 |doi=10.1007/s00253-004-1568-8}}</ref><ref>{{cite journal |vauthors=Ban K, Kaieda M, Matsumoto T, Kondo A, Fukuda H |title=Whole cell biocatalyst for biodiesel fuel production utilizing Rhizopus oryzae cells immobilized within biomass support particles|journal=Biochem Eng J|volume=8|issue=1|pages=39–43|year=2001|pmid=11356369 |doi=10.1016/S1369-703X(00)00133-9}}</ref> 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,<ref>{{cite journal |doi=10.1016/j.jclepro.2007.07.003 |title=A life-cycle comparison between inorganic and biological catalysis for the production of biodiesel |journal=Journal of Cleaner Production |volume=16 |issue=13 |pages=1368–78 |year=2008 |last1=Harding |first1=K.G |last2=Dennis |first2=J.S |last3=von Blottnitz |first3=H |last4=Harrison |first4=S.T.L }}</ref> 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.<ref>{{cite journal |doi=10.1021/ma301178k |title=Enzyme-Catalyzed Polymerization of End-Functionalized Polymers in a Microreactor |journal=Macromolecules |volume=45 |issue=17 |pages=7000–8 |year=2012 |last1=Bhangale |first1=Atul S |last2=Beers |first2=Kathryn L |last3=Gross |first3=Richard A }}</ref><ref>{{cite journal |doi=10.1021/ja111346c |pmid=21438577 |title=Continuous Flow Enzyme-Catalyzed Polymerization in a Microreactor |journal=Journal of the American Chemical Society |volume=133 |issue=15 |pages=6006–11 |year=2011 |last1=Kundu |first1=Santanu |last2=Bhangale |first2=Atul S |last3=Wallace |first3=William E |last4=Flynn |first4=Kathleen M |last5=Guttman |first5=Charles M |last6=Gross |first6=Richard A |last7=Beers |first7=Kathryn L }}</ref> 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.<ref>{{cite web|title=Lipase - TheTest|url=http://labtestsonline.org/understanding/analytes/lipase/tab/test/|work=Lab Tests Online|accessdate=12 May 2014}}</ref> Measured serum lipase values may vary depending on the method of analysis.

==Medical use==
Lipase can also assist in the breakdown of [[fat]]s into [[lipids]] in those undergoing [[pancreatic enzyme replacement therapy]] (PERT). It is a key component in [[Sollpura (Liprotamase)]].<ref>"Anthera Pharmaceuticals - Sollpura." Anthera Pharmaceuticals - Sollpura. N.p., n.d. Web. 21 July 2015. <http://www.anthera.com/pipeline/science/sollpura.html>.</ref><ref>{{cite journal |doi=10.3109/14756366.2010.525509 |pmid=21028941 |title=Pancreatic lipase inhibition activity of trilactone terpenes of ''Ginkgo biloba'' |journal=Journal of Enzyme Inhibition and Medicinal Chemistry |volume=26 |issue=4 |pages=453–9 |year=2010 |last1=Bustanji |first1=Yasser |last2=Al-Masri |first2=Ihab M |last3=Mohammad |first3=Mohammad |last4=Hudaib |first4=Mohammad |last5=Tawaha |first5=Khaled |last6=Tarazi |first6=Hamada |last7=Alkhatib |first7=Hatim S }}</ref>

==Additional images==
<gallery>
Image:Ester-general.png|General formula of a carboxylate [[ester]]
Image:Glycerine chemical structure.png|[[Glycerol]]
</gallery>

==See also==
*[[Alpha toxin (disambiguation)|Alpha toxin]]
*[[Lysosomal acid lipase deficiency]]
*[[Peripheral membrane protein]]s
*[[Phospholipase A (disambiguation)|Phospholipase A]]
*[[Phospholipase C]]
*[[Triglyceride lipase]]
* [[Phospholipase A2]]
* [[Outer membrane phospholipase A1]]
* [[Patatin-like phospholipase]]

==References==
{{Reflist|2}}

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==
* {{MeshName|Lipase}}

{{Esterases}}
{{Enzymes}}
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[[Category:Hydrolases]]
[[Category:Peripheral membrane proteins]]
[[Category:EC 3.1]]

Revision as of 20:37, 19 November 2018

lipase is kool and it makes u kool

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