Lipase - *i+ipedia, the free encyclopedia

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Lipase
)rom *i+ipedia, the free encyclopedia

Lipase is an en-yme that cataly-es the hydrolysis of fats .1/ (lipids). Lipases are a su$class 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, li0ing organisms. enes encoding lipases are e0en present .2/.1/ in certain 0iruses. 2ost lipases act at a specific position on the glycerol $ac+$one of lipid su$strate (A1, A2 or A1)(small intestine). )or e%ample, .4/ human pancreatic lipase (3PL), #hich is the main en-yme that $rea+s do#n dietary fats in the human digesti0e system, con0erts triglyceride su$strates found in ingested oils to monoglycerides and t#o fatty acids. 5e0eral other types of lipase acti0ities e%ist in nature, such as .6/ .7/ phospholipases and sphingomyelinases, ho#e0er these are usually treated separately from 8con0entional8 lipases. 5ome lipases are e%pressed and secreted $y pathogenic organisms during the infection. 'n particular, Candida albicans has a large num$er of different lipases, possi$ly reflecting $road lipolytic acti0ity, #hich may contri$ute to the persistence and 0irulence of .9/ C. albicans in human tissue.
A computer-generated image of a type of pancreatic lipase (PLRP2) from the guinea pig. PDB 1 PL (http!""###.rcs$.org "pd$"e%plore "e%plore.do&structure'd(1 PL).

Contents
1 2 1 4 6 7 9 : ; 5tructure and catalytic mechanism Physiological distri$ution 3uman lipases 'ndustrial uses 5ource Additional images 5ee also References <%ternal lin+s

Structure and catalytic mechanism

Although a di0erse array of genetically distinct lipase en-ymes are found in nature, and represent se0eral types of protein folds and catalytic mechanisms, most are $uilt on an .:/.;/.1=/ .11/ alpha"$eta hydrolase fold (see image ) and employ a chymotrypsin-li+e hydrolysis mechanism in0ol0ing a serine nucleophile, an acid residue (usually aspartic acid), and a .12/.11/ histidine.

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Physiological distribution
Lipases are in0ol0ed in di0erse $iological processes ranging from routine meta$olism of dietary .14/ .16/ triglycerides to cell signaling and inflammation. >hus, some lipase acti0ities are confined to specific compartments #ithin cells #hile others #or+ in e%tracellular spaces. 'n the e%ample of lysosomal lipase, the en-yme is confined #ithin an organelle called the lysosome. ?ther lipase en-ymes, such as pancreatic lipases, are secreted into e%tracellular spaces #here they ser0e to process dietary lipids into more simple forms that can $e more easily a$sor$ed and transported throughout the $ody. )ungi and $acteria may secrete lipases to facilitate nutrient a$sorption from the e%ternal medium (or in e%amples of pathogenic micro$es, to promote in0asion of a ne# host). @ertain #asp and $ee 0enoms contain phospholipases that enhance the 8$iological payload8 of inAury and inflammation deli0ered $y a sting. As $iological mem$ranes are integral to li0ing cells and are largely composed of phospholipids, lipases play important roles in cell $iology. 2alasse-ia glo$osa, a fungus that is thought to $e the cause of human dandruff, uses lipase to $rea+ do#n se$um into oleic acid and increase s+in cell production, causing dandruff.
.17/

Human lipases
>he main lipases of the human digesti0e system are human pancreatic lipase (3PL) and pancreatic lipase related protein 2 (PLRP2), #hich are secreted $y the pancreas. 3umans also ha0e se0eral other related en-ymes, including hepatic lipase (3L), endothelial lipase, and lipoprotein lipase. Bot all of these lipases function in the gut (see ta$le).

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Name $ile salt dependent lipase

Gene &

Location pancreas, $reast mil+

Description aids in the digestion of fats 'n order to e%hi$it optimal en-yme acti0ity in the gut lumen, 3PL reCuires another protein, colipase, #hich is also secreted $y the pancreas.
.19/

Disorder

pancreatic PNLIP (http://www.genenames.org lipase /data/hgnc_data.php?match=PNLIP)

digesti0e Auice

lysosomal lipase

LIP (http://www.genenames.org /data/hgnc_data.php?match=LIP )

interior space of organelle! lysosome

Also referred to as lysosomal acid lipase (LAL or L'PA) or acid cholesteryl ester hydrolase

@holesteryl ester storage disease (@<5D) and *olman disease are $oth caused $y mutations in the gene encoding lysosomal lipase.
.1:/

hepatic lipase

LIPC (http://www.genenames.org /data/hgnc_data.php?match=LIPC)

3epatic lipase acts on the remaining lipids carried on endothelium lipoproteins in the $lood to regenerate LDL (lo# density lipoprotein). Lipoprotein lipase functions in the $lood to endothelium act on triacylglycerides carried on DLDL (0ery lo# Lipoprotein lipase deficiency is caused $y mutations in the

LPL (http://www.genenames.org lipoprotein /data/hgnc_data.php?match=LPL) or lipase 8L'PD8

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density lipoprotein) so that cells can ta+e up the freed fatty acids. hormonesensiti0e lipase LIP! (http://www.genenames.org /data/hgnc_data.php?match=LIP!) intracellular -

gene encoding lipoprotein lipase.

.1;/.2=/

gastric lipase

LIP" (http://www.genenames.org /data/hgnc_data.php?match=LIP")

digesti0e Auice

)unctions in the infant at a near-neutral p3 to aid in the digestion of lipids -

endothelial LIP# (http://www.genenames.org lipase /data/hgnc_data.php?match=LIP#)

endothelium -

pancreatic PNLIP$P% (http://www.genenames.org digesti0e lipase /data/hgnc_data.php?match=PNLIP$P%) Auice related or 8PLRP28 protein 2

pancreatic PNLIP$P& (http://www.genenames.org digesti0e lipase /data/hgnc_data.php?match=PNLIP$P&) Auice related or 8PLRP18 protein 1

Pancreatic lipase related protein 1 is 0ery similar to PLRP2 and 3PL $y amino acid seCuence (all three genes pro$a$ly arose 0ia gene duplication of a single ancestral pancreatic lipase gene). 3o#e0er, PLRP1 is de0oid of detecta$le lipase acti0ity and its function remains un+no#n, e0en though it is conser0ed in other mammals.
.21/.22/

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lingual lipase

&

digesti0e Auice

Acti0e at gastric p3 le0els. ?ptimum p3 is a$out 1.6-7. 5creted $y the Parotid and <$nerEs glands at the $ac+ of the tongue.

?ther lipases include LIP' (http://www.genenames.org/data/hgnc_data.php?match=LIP'), LIPI (http://www.genenames.org/data/hgnc_data.php?match=LIPI), LIP( (http://www.genenames.org/data/hgnc_data.php?match=LIP(), LIP) (http://www.genenames.org/data/hgnc_data.php?match=LIP)), LIP* (http://www.genenames.org/data/hgnc_data.php?match=LIP*), LIPN (http://www.genenames.org/data/hgnc_data.php?match=LIPN), *#LL (http://www.genenames.org/data/hgnc_data.php?match=*#LL), + #L (http://www.genenames.org/data/hgnc_data.php?match=+ #L ), + #L, (http://www.genenames.org/data/hgnc_data.php?match=+ #L,), and C!L (http://www.genenames.org/data/hgnc_data.php?match=C!L). >here also are a di0erse array of phospholipases, $ut these are not al#ays classified #ith the other lipases.

Industrial uses
Lipases ser0e important roles in human practices as ancient as yogurt and cheese fermentation. 3o#e0er, lipases are also $eing e%ploited as cheap and 0ersatile catalysts to degrade lipids in more modern applications. )or instance, a $iotechnology company has $rought recom$inant lipase en-ymes to mar+et for use in applications such as $a+ing, laundry detergents and e0en .21/ .24/.26/ as $iocatalysts in alternati0e energy strategies to con0ert 0egeta$le oil into fuel. 3igh en-yme acti0ity lipase can replace traditional catalyst in processing $iodiesel, this en-yme is more en0ironmental and safe. 'ndustrial applicaton of lipases reCuires process intensification .27/ .29/ for continuous processing using tools li+e continuous flo# microreactors at small scale.

Source
Lipases are generally animal sourced, $ut can also $e sourced micro$ially. 5erum lipase 0alues .2:/ in the human $ody range normally from =-17= F"L.

Additional images

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eneral formula of a car$o%ylate ester

lycerol

See also
Alpha to%in Lysosomal acid lipase deficiency Peripheral mem$rane proteins Phospholipase A Phospholipase @ >riglyceride lipase

References
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26. ul-ar, Bio-degradation of hydrocar$ons using different $acterial and fungal species. Pu$lished in international conference on $iotechnology and neurosciences. @F5A> (cochin uni0ersity of science and technology), 2==4

+,ternal lin-s
Lipase (http!""###.nlm.nih.go0"cgi"mesh"2=11"2BQcgi&mode(Rterm(Lipase) at the F5 Bational Li$rary of 2edicine 2edical 5u$Aect 3eadings (2e53) 5electi0e 'nhi$itors of 2onoacylglycerol Lipase as a >reatment for Beurological Disorders 2==4-719 (http!""logi+$ase.com"#e$site"techprofile.cfm&licid(;4=) F2ich ?rientation of Proteins in 2em$ranes 4amilies/s/per4amil-567 (http://opm.phar./mich.ed//4amilies.php?s/per4amil-=67) - Phospholipases A2 F2ich ?rientation of Proteins in 2em$ranes 4amilies/s/per4amil-5%6 (http://opm.phar./mich.ed//4amilies.php?s/per4amil-=%6) - ?uter mem$rane phospholipase A F2ich ?rientation of Proteins in 2em$ranes 4amilies/s/per4amil-5&89 (http://opm.phar./mich.ed//4amilies.php?s/per4amil-=&89) - @ytosolic phospholipase A2 and patatin F2ich ?rientation of Proteins in 2em$ranes 4amilies/s/per4amil-5&%:

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(http://opm.phar./mich.ed//4amilies.php?s/per4amil-=&%:) - Bacterial and mammalian phospholipases @ F2ich ?rientation of Proteins in 2em$ranes 4amilies/s/per4amil-5;; (http://opm.phar./mich.ed//4amilies.php?s/per4amil-=;;) - S-to%in (a $acterial phospholipase @) Retrie0ed from 8http!""en.#i+ipedia.org"#"inde%.php&title(LipaseRoldid(6::1944648 @ategories! 3ydrolases Peripheral mem$rane proteins <@ 1.1 >his page #as last modified on 2; Decem$er 2=11 at =7!12. >e%t is a0aila$le under the @reati0e @ommons Attri$ution-5hareAli+e LicenseO additional terms may apply. By using this site, you agree to the >erms of Fse and Pri0acy Policy. *i+ipediaT is a registered trademar+ of the *i+imedia )oundation, 'nc., a non-profit organi-ation.

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