Jump to content

Lipase: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
Ionescuac (talk | contribs)
458 edits
Revert edit to #128460210
Jpkamil (talk | contribs)
198 edits
added new industrial uses section
Line 54: Line 54:


There also are a diverse array of [[phospholipase]]s, but these are not always classified with the other lipases.
There also are a diverse array of [[phospholipase]]s, but these are not always classified with the other lipases.

==Industrial Uses==
Lipases from fungi and bacteria are used in industrial applications as diverse as yogurt and cheese fermentation to as ingredients in laundry detergents. Furthermore, fungal lipases are being explored in alternative fuel strategies to convert vegetable oil into fuel. <ref>{{cite journal |author=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}}</ref><ref>{{cite journal |author=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}}</ref>


==Additional images==
==Additional images==

Revision as of 06:01, 11 May 2007

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

A lipase is a water-soluble enzyme that catalyzes the hydrolysis of ester bonds in water–insoluble, lipid substrates[1].

Lipases are ubiquitous throughout living organisms, and genes encoding lipases are even present in certain viruses. [2][3]

Function

Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3).

In the example of human pancreatic lipase (HPL)[4], which is the main enzyme responsible for breaking down fats in the human digestive system, a lipase acts to convert triglyceride substrates found in oils from food to monoglycerides and free fatty acids.

Myriad other lipase activities exist in nature, especially when the phospholipases[5] and sphingomyelinases[6] are considered.

Structure

While a diverse array of genetically distinct lipase enzymes are found in nature, and represent distinct types of protein folds and catalytic mechanisms, most are built on an alpha/beta hydrolase fold [7][8][9] (see image[10]) and employ a chymotrypsin-like hydrolysis mechanism involving a serine nucleophile, an acid residue (usually aspartic acid), and a histidine[11][12].

Location of action

Some lipases work within the interior spaces of living cells to degrade lipids.

  • In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
  • Other lipase enzymes, such as pancreatic lipases, are found in the spaces outside of cells and have roles in the metabolism, absorption and transport of lipids throughout the body.

As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology.

Furthermore, lipases are involved in diverse biological processes ranging from routine metabolism of dietary triglycerides to cell signaling[13] and inflammation[14].

Types in humans

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

Name Gene Description Disorder
pancreatic lipase PNLIP In order to exhibit optimal enzyme activity in the gut lumen, HPL requires another protein, colipase, which is also secreted by the pancreas[15]. -
lysosomal lipase LIPA 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.[16]
hepatic lipase LIPC Hepatic lipase acts on the remaining lipids carried on lipoproteins in the blood to regenerate LDL (low density lipoprotein). -
lipoprotein lipase LPL or "LIPD" 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.[17] [18]
hormone-sensitive lipase LIPE - -
gastric lipase LIPF - -
endothelial lipase LIPG - -
pancreatic lipase related protein 2 PNLIPRP2 or "PLRP2" - -
pancreatic lipase related protein 1 PNLIPRP1 or "PLRP1" Pancreatic lipase related protein 1 is very similar to PLRP2 and HPL 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[19][20]. -

Other lipases include LIPH, LIPI, LIPJ, LIPK, LIPM, and LIPN.

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

Industrial Uses

Lipases from fungi and bacteria are used in industrial applications as diverse as yogurt and cheese fermentation to as ingredients in laundry detergents. Furthermore, fungal lipases are being explored in alternative fuel strategies to convert vegetable oil into fuel. [21][22]

Additional images

References

  1. ^ Svendsen A (2000). "Lipase protein engineering". Biochim Biophys Acta. 1543 (2): 223–228. PMID 11150608.
  2. ^ Afonso C, Tulman E, Lu Z, Oma E, Kutish G, Rock D (1999). "The genome of Melanoplus sanguinipes entomopoxvirus". J Virol. 73 (1): 533–52. PMID 9847359.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Winkler FK, D'Arcy A, and W Hunziker (1990). "Structure of human pancreatic lipase". Nature. 343 (6260): 771–774. PMID 2106079. {{cite journal}}: Cite has empty unknown parameter: |1= (help)CS1 maint: multiple names: authors list (link)
  5. ^ Diaz, B.L., and J. P. Arm. (2003). "Phospholipase A(2)". Prostaglandins Leukot Essent Fatty Acids. 2–3: 87–97. PMID 12895591. {{cite journal}}: Cite has empty unknown parameter: |1= (help)CS1 maint: multiple names: authors list (link)
  6. ^ Goñi F, Alonso A (2002). "Sphingomyelinases: enzymology and membrane activity". FEBS Lett. 531 (1): 38–46. PMID 12401200.
  7. ^ Schrag J, Cygler M. "Lipases and alpha/beta hydrolase fold". Methods Enzymol. 284: 85–107. PMID 9379946.
  8. ^ Winkler FK, D'Arcy A, and W Hunziker (1990). "Structure of human pancreatic lipase". Nature. 343 (6260): 771–774. PMID 2106079. {{cite journal}}: Cite has empty unknown parameter: |1= (help)CS1 maint: multiple names: authors list (link)
  9. ^ Egmond, M. R., and C. J. van Bemmel (1997). "Impact of Structural Information on Understanding of Lipolytic Function". Methods Enzymol. 284: 119–129. PMID 9379930.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  10. ^ Withers-Martinez C, Carriere F, Verger R, Bourgeois D, and C Cambillau (1996). "A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig". Structure. 4 (11): 1363–74. PMID 8939760.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  11. ^ Brady, L., A. M. Brzozowski, Z. S. Derewenda, E. Dodson, G. Dodson, S. Tolley, J. P. Turkenburg, L. Christiansen, B. Huge-Jensen, L. Norskov, and; et al. (1990). "A serine protease triad forms the catalytic centre of a triacylglycerol lipase". Nature. 343 (6260): 767–70. PMID 2304552. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  12. ^ Lowe ME (1992). "The catalytic site residues and interfacial binding of human pancreatic lipase". J Biol Chem. 267 (24): 17069–73. PMID 1512245.
  13. ^ Spiegel S, Foster D, and R Kolesnick (1996). "Signal transduction through lipid second messengers". Curr Opin Cell Biol. 8 (2): 159–67. PMID 8791422.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  14. ^ Tjoelker LW, Eberhardt C, Unger J, Trong HL, Zimmerman GA, McIntyre TM, Stafforini DM, Prescott SM, and PW Gray (1995). "Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad". J Biol Chem. 270 (43): 25481–7. PMID 7592717.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  15. ^ Lowe ME (2002). "The triglyceride lipases of the pancreas". J Lipid Res. 43 (12): 2007–16. PMID 12454260.
  16. ^ http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=278000
  17. ^ http://ghr.nlm.nih.gov/condition=lipoproteinlipasedeficiencyfamilial
  18. ^ Gilbert B, Rouis M, Griglio S, de Lumley L, Laplaud P. "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". Ann Genet. 44 (1): 25–32. PMID 11334614.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  19. ^ 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. PMID 9605548.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  20. ^ 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. PMID 9748646.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  21. ^ Gupta R, Gupta N, Rathi P (2004). "Bacterial lipases: an overview of production, purification and biochemical properties". Appl Microbiol Biotechnol. 64 (6): 763–81. PMID 14966663.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  22. ^ 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. PMID 11356369. {{cite journal}}: Cite has empty unknown parameter: |1= (help)CS1 maint: multiple names: authors list (link)

See also

Retrieved from "https://en.wikipedia.org/w/index.php?title=Lipase&oldid=130031629"