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Lipase family functions
Lipases are water-soluble enzymes that catalyze the hydrolysis of ester chemical bonds
in water-insoluble lipid substrates. Lipases are widely distributed in animals, plants
and prokaryotes. The lipase family consists of triglyceride lipases, phospholipases and
sphingomyelinases. By the place of action lipases can be divided on 3 sub-classes:
extracellular, membrane and intracellular lipases.
Extracellular lipases are represented by Lipase, family member M
(LIPM ), Lipase, family member K
(LIPK ) and Lipase, family member N
(Lipn ). These lipases convert Triacylglycerols
extracellular region into Carboxylic acids extracellular
region and 1,2-Diacyglycerol extracellular
region . Furthermore, the function of these lipases is necessary for
keratinocyte differentiation [1 ].
Membrane lipases are represented by phospholipases: Lipase, member I
(LIPI ) and Lipase, member H
(LIPH ). They catalyze conversion of
Phosphatidic acid into Free fatty
acid and 2-Acyl
lysophosphatidic acid , which further participates in
phospholipid metabolism [2 ], [3 ].
The most abundant intracellular lipases include: Lipoprotein lipase
(LPL ), Lipase, hepatic (LIPC
(HL) ), Lipase, endothelial
(LIPG ) and Lipase, hormone-sensitive
(LIPE ). All of them catalyze the hydrolysis of
triacylglycerol resulting in the formation of
1,2-diacylglycerol . LIPC (HL) ,
LIPG and LIPE also convert
1,2-diacylglycerol into 2-monoacyl
glycerol and the latter into glycerol , which
participates in triacylglycerol metabolism [4 ], [5 ], [6 ], [7 ], [8 ].
In addition, LPL catalyses the conversion of
1,2-diacylglycerol into
1-acyl-glycerol and Free fatty
acid and subsequent formation of Free fatty
acid and glycerol form
1-acyl-glycerol [4 ], [9 ].
Toulza E, Mattiuzzo NR, Galliano MF, Jonca N, Dossat C, Jacob D, de Daruvar A, Wincker P, Serre G, Guerrin M
Large-scale identification of human genes implicated in epidermal barrier function.
Genome biology 2007;8(6):R107
Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H
A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.
The Journal of biological chemistry 2002 Sep 13;277(37):34254-63
Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H
Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.
The Journal of biological chemistry 2003 Dec 5;278(49):49438-47
Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S
Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241.
The Journal of biological chemistry 1992 Feb 25;267(6):4161-5
Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T
Cloning of a unique lipase from endothelial cells extends the lipase gene family.
The Journal of biological chemistry 1999 May 14;274(20):14170-5
Carriere F, Renou C, Lopez V, De Caro J, Ferrato F, Lengsfeld H, De Caro A, Laugier R, Verger R
The specific activities of human digestive lipases measured from the in vivo and in vitro lipolysis of test meals.
Gastroenterology 2000 Oct;119(4):949-60
McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ
Characterization of the lipolytic activity of endothelial lipase.
Journal of lipid research 2002 Jun;43(6):921-9
Miles JM, Park YS, Walewicz D, Russell-Lopez C, Windsor S, Isley WL, Coppack SW, Harris WS
Systemic and forearm triglyceride metabolism: fate of lipoprotein lipase-generated glycerol and free fatty acids.
Diabetes 2004 Mar;53(3):521-7
van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C
Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis.
The Journal of biological chemistry 1994 Feb 11;269(6):4626-33
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