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Lipase

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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 thus comprise 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]

Function

Most lipases act at a specific position on the glycerol backbone of 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 of 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 several 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]. Many lipases that are produced by Gram-negative bacteria require a dedicated helper protein, a lipase-specific foldase, to obtain their native, fully folded and biologically active conformation.

Physiological distribution

Lipases are involved in diverse biological processes ranging from routine metabolism of dietary triglycerides to cell signaling[13] and inflammation[14]. Thus, some lipase activities are confined to specific compartments within cells 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 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 phospholipases that enhance the "biological payload" of injury and inflammation delivered by a sting.

Lipases of humans

The main lipases of the human 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 Location Description Disorder
pancreatic lipase PNLIP digestive juice In order to exhibit optimal enzyme activity in the gut lumen, HPL requires another protein, colipase, which is also secreted by the pancreas[15]. If pancreatic lipase levels get too high, the patient will develop pancreatitis, and his pancreas will fail
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.[16]
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.[17] [18]
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 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]. -
lingual lipase ? digestive juice - -

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 from fungi and bacteria 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 [21] in alternative energy strategies to convert vegetable oil into fuel. [22][23]

Additional images

See also

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. doi:10.1038/343771a0. PMID 2106079.{{cite journal}}: 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. doi:10.1016/S0952-3278(03)00069-3. PMID 12895591.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Goñi F, Alonso A (2002). "Sphingomyelinases: enzymology and membrane activity". FEBS Lett. 531 (1): 38–46. doi:10.1016/S0014-5793(02)03482-8. PMID 12401200.
  7. ^ Schrag J, Cygler M (1997). "Lipases and alpha/beta hydrolase fold". Methods Enzymol. 284: 85–107. doi:10.1016/S0076-6879(97)84006-2. PMID 9379946.
  8. ^ Winkler FK, D'Arcy A, and W Hunziker (1990). "Structure of human pancreatic lipase". Nature. 343 (6260): 771–774. doi:10.1038/343771a0. PMID 2106079.{{cite journal}}: 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. doi:10.1016/S0076-6879(97)84008-6. 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. doi:10.1016/S0969-2126(96)00143-8. 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. doi:10.1038/343767a0. 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. doi:10.1016/S0955-0674(96)80061-5. 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. doi:10.1074/jbc.270.43.25481. PMID 7592717.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  15. ^ Lowe ME (2002). "The triglyceride lipases of the pancreas". J Lipid Res. 43 (12): 2007–16. doi:10.1194/jlr.R200012-JLR200. PMID 12454260.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  16. ^ Omim - Wolman Disease
  17. ^ Familial lipoprotein lipase deficiency - Genetics Home Reference
  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. doi:10.1093/protein/11.2.135. 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. ^ Guo Z, Xu X (2005). "New opportunity for enzymatic modification of fats and oils with industrial potentials". Org Biomol Chem. 3 (14): 2615–9. doi:10.1039/b506763d. PMID 15999195.
  22. ^ Gupta R, Gupta N, Rathi P (2004). "Bacterial lipases: an overview of production, purification and biochemical properties". Appl Microbiol Biotechnol. 64 (6): 763–81. doi:10.1007/s00253-004-1568-8. PMID 14966663.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  23. ^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

{Esterases}}

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