Lipase - wikipedia Lipase A computer - generated image of a type of pancreatic lipase ( PLRP2 ) from the guinea pig. PDB : 1GPL ​. A lipase ( / ˈlaɪpeɪs /, / ˈlɪpeɪs /, / - peɪz / ) is any enzyme that catalyzes the hydrolysis of fats ( lipids ). Lipases are 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. Most lipases act at a specific position on the glycerol backbone of a lipid substrate ( A1, A2 or A3 ) ( small intestine ). For example, human pancreatic lipase ( HPL ), which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids. Several other types of lipase activities exist in nature, such as phospholipases and sphingomyelinases, 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 - lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue. Contents 1 Structure and catalytic mechanism 2 Physiological distribution 3 Human lipases 4 Industrial uses 5 Diagnostic use 6 Medical use 7 Additional images 8 See also 9 References 10 External links Structure and catalytic mechanism Although a diverse array of genetically distinct lipase enzymes are found in nature ; and, they represent several types of protein folds and catalytic mechanisms, most of them are built on an alpha / beta hydrolase fold 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 ). Physiological distribution Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling and inflammation. 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 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. 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. 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 ). Name Gene Location Description Disorder bile salt - dependent lipase bsdl pancreas, breast milk aids in the digestion of fats pancreatic lipase 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. 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. 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. 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. - 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. There also are a diverse array of phospholipases, 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 biocatalysts in alternative energy strategies to convert vegetable oil into fuel. 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, 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. 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. Measured serum lipase values may vary depending on the method of analysis. Medical use Lipase can also assist in the breakdown of fats into lipids in those undergoing pancreatic enzyme replacement therapy ( PERT ). It is a key component in Sollpura ( Liprotamase ). Additional images General formula of a carboxylate ester Glycerol See also Alpha toxin Lysosomal acid lipase deficiency Peripheral membrane proteins Phospholipase A Phospholipase C Triglyceride lipase References Jump up ^ Svendsen A ( 2000 ). `` Lipase protein engineering ''. Biochim Biophys Acta. 1543 ( 2 ) : 223 -- 228. doi : 10.1016 / S0167 - 4838 ( 00 ) 00239 - 9. PMID 11150608. Jump up ^ Afonso C, Tulman E, Lu Z, Oma E, Kutish G, Rock D ( 1999 ). `` The Genome of Melanoplus sanguinipes Entomologists ''. J Virol. 73 ( 1 ) : 533 -- 52. PMC 103860. PMID 9847359. Jump up ^ 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. Jump up ^ Winkler FK ; D'Arcy A ; W Hunziker ( 1990 ). `` Structure of human pancreatic lipase ''. Nature. 343 ( 6260 ) : 771 -- 774. doi : 10.1038 / 343771a0. PMID 2106079. Jump up ^ Diaz, B.L. ; J.P. Arm. ( 2003 ). `` Phospholipase A ( 2 ) ''. Prostaglandins Leukot Essent Fatty Acids. 69 ( 2 -- 3 ) : 87 -- 97. doi : 10.1016 / S0952 - 3278 ( 03 ) 00069 - 3. PMID 12895591. Jump up ^ 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. Jump up ^ Hube B, Stehr F, Bossenz M, Mazur A, Kretschmar M, Schafer W ( 2000 ). `` Secreted lipases of Candida albicans : cloning, characterisation and expression analysis of a new gene family with at least ten members ''. Arch. Microbiol. 174 ( 5 ) : 362 -- 374. doi : 10.1007 / s002030000218. PMID 11131027. Jump up ^ Winkler FK ; D'Arcy A ; W Hunziker ( 1990 ). `` Structure of human boob pancreatic lipase ''. Nature. 343 ( 6260 ) : 771 -- 774. doi : 10.1038 / 343771a0. PMID 2106079. Jump up ^ Schrag J, Cygler M ( 1997 ). `` Lipases and alpha / beta hydrolase fold ''. Methods Enzymol. Methods in Enzymology. 284 : 85 -- 107. doi : 10.1016 / S0076 - 6879 ( 97 ) 84006 - 2. ISBN 978 - 0 - 12 - 182185 - 2. PMID 9379946. Jump up ^ Egmond, M.R. ; C.J. van Bemmel ( 1997 ). `` Impact of Structural Information on Understanding of Lipolytic Function ''. Methods Enzymol. Methods in Enzymology. 284 : 119 -- 129. doi : 10.1016 / S0076 - 6879 ( 97 ) 84008 - 6. ISBN 978 - 0 - 12 - 182185 - 2. PMID 9379930. Jump up ^ Withers - Martinez C ; Carriere F ; Verger R ; Bourgeois D ; 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. Jump up ^ Brady, L. ; A.M. Brzozowski ; Z.S. Derewenda ; E. Dodson ; G. Dodson ; S. Tolley ; J.P. Turkenburg ; L. Christiansen ; B. Huge - Jensen ; L. Norskov ; 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. Jump up ^ Lowe ME ( 1992 ). `` The catalytic site residues and interfacial binding of human pancreatic lipase ''. J Biol Chem. 267 ( 24 ) : 17069 -- 73. PMID 1512245. Jump up ^ Spiegel S ; Foster D ; R Kolesnick ( 1996 ). `` Signal transduction through lipid second messengers ''. Current Opinion in Cell Biology. 8 ( 2 ) : 159 -- 67. doi : 10.1016 / S0955 - 0674 ( 96 ) 80061 - 5. PMID 8791422. Jump up ^ Tjoelker LW ; Eberhardt C ; Unger J ; Trong HL ; Zimmerman GA ; McIntyre TM ; Stafforini DM ; Prescott SM ; 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. Jump up ^ Genetic Code of Dandruff Cracked - BBC News Jump up ^ Lowe ME ( 2002 ). `` The triglyceride lipases of the pancreas ''. J Lipid Res. 43 ( 12 ) : 2007 -- 16. doi : 10.1194 / jlr. R200012 - JLR200. PMID 12454260. Jump up ^ Omim - Wolman Disease Jump up ^ Familial lipoprotein lipase deficiency - Genetics Home Reference Jump up ^ Gilbert B, Rouis M, Griglio S, de Lumley L, Laplaud P ( 2001 ). `` 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. doi : 10.1016 / S0003 - 3995 ( 01 ) 01037 - 1. PMID 11334614. Jump up ^ 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. 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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 ), 2004 External links Lipase at the US National Library of Medicine Medical Subject Headings ( MeSH ) UMich Orientation of Proteins in Membranes families / superfamily - 90 - Phospholipases A2 UMich Orientation of Proteins in Membranes families / superfamily - 29 - Outer membrane phospholipase A UMich Orientation of Proteins in Membranes families / superfamily - 134 - Cytosolic phospholipase A2 and patatin UMich Orientation of Proteins in Membranes families / superfamily - 126 - Bacterial and mammalian phospholipases C UMich Orientation of Proteins in Membranes families / superfamily - 88 - α - toxin ( a bacterial phospholipase C ) Lipase at Lab Tests Online Hydrolase : esterases ( EC 3.1 ) 3.1. 1 : Carboxylic ester hydrolases Cholinesterase Acetylcholinesterase Butyrylcholinesterase Pectinesterase 6 - phosphogluconolactonase PAF acetylhydrolase Lipase Bile salt - dependent Gastric / Lingual Pancreatic Lysosomal Hormone - sensitive Endothelial Hepatic Lipoprotein Monoacylglycerol Diacylglycerol Phospholipase A1 A2 3.1. 2 : Thioesterase Palmitoyl protein thioesterase Ubiquitin carboxy - terminal hydrolase L1 4 - hydroxybenzoyl - CoA thioesterase 3.1. 3 : Phosphatase Alkaline phosphatase ALPI ALPL ALPP Acid phosphatase ( Prostatic ) / Tartrate - resistant acid phosphatase / Purple acid phosphatases Nucleotidase Glucose 6 - phosphatase Fructose 1, 6 - bisphosphatase Calcineurin Protein phosphatase PP2A OCRL Pyruvate dehydrogenase phosphatase Fructose 6 - P, 2 - kinase : fructose 2, 6 - bisphosphatase PTEN Phytase Inositol - phosphate phosphatase IMPA1, IMPA2, IMPA3 Protein phosphatase : Protein tyrosine phosphatase Protein serine / threonine phosphatase Dual - specificity phosphatase 3.1. 4 : Phosphodiesterase Autotaxin Phospholipase Sphingomyelin phosphodiesterase PDE1 PDE2 PDE3 PDE4A / PDE4B PDE5 Lecithinase ( Clostridium perfringens alpha toxin ) Cyclic nucleotide phosphodiesterase 3.1. 6 : Sulfatase arylsulfatase Arylsulfatase A Arylsulfatase B Arylsulfatase E Steroid sulfatase Galactosamine - 6 sulfatase Iduronate - 2 - sulfatase N - acetylglucosamine - 6 - sulfatase Nuclease ( includes deoxyribonuclease and ribonuclease ) 3.1. 11 - 16 : Exonuclease Exodeoxyribonuclease RecBCD Exoribonuclease Oligonucleotidase 3.1. 21 - 31 : Endonuclease Endodeoxyribonuclease Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease Endoribonuclease RNase III RNase H 2A 2B 2C RNase P RNase A 4 / 5 RNase T1 RNA - induced silencing complex either deoxy - or ribo - Aspergillus nuclease S1 Micrococcal nuclease Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics Types EC1 Oxidoreductases ( list ) EC2 Transferases ( list ) EC3 Hydrolases ( list ) EC4 Lyases ( list ) EC5 Isomerases ( list ) EC6 Ligases ( list ) Common for blood tests ( CPT 82000 -- 84999 ) Electrolytes Sodium Potassium Chloride Calcium Renal function Creatinine Urea BUN - to - creatinine ratio Plasma osmolality Serum osmolal gap Acid - base Anion gap Arterial blood gas Base excess Bicarbonate CO content Iron tests Ferritin Serum iron Transferrin saturation Total iron - binding capacity Transferrin Transferrin receptor Hormones ACTH stimulation test Thyroid function tests Thyroid - stimulating hormone Metabolism Blood lipids Cardiovascular Cardiac marker Troponin test CPK - MB test Lactate dehydrogenase Myoglobin Glycogen phosphorylase isoenzyme BB Liver function tests Proteins Human serum albumin Serum total protein ALP transaminases ALT AST AST / ALT ratio Bilirubin Unconjugated Conjugated Pancreas Amylase Lipase Pancreatic lipase NDL : 00576465 Molecular and Cellular Biology portal Retrieved from `` https://en.wikipedia.org/w/index.php?title=Lipase&oldid=800137751 '' Categories : Hydrolases Peripheral membrane proteins EC 3.1 Talk Contents About Wikipedia Bosanski Català Čeština Dansk Deutsch Español فارسی Français Gaeilge Galego 한국어 हिन्दी Bahasa Indonesia Italiano עברית Қазақша Кыргызча Latviešu Bahasa Melayu Nederlands 日本 語 Norsk Oʻzbekcha / ўзбекча ਪੰਜਾਬੀ Polski Português Русский Simple English Slovenščina Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska தமிழ் Türkçe Українська 中文 Edit links This page was last edited on 11 September 2017, at 18 : 30. 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Question: give two places in the body that produce lipases
Answer: pancreas