Pancreatic lipase family

Pfam_box
Symbol = Lipase
Name =

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width =250
caption =Complex of human pancreatic lipase with colipase
Pfam= PF00151
InterPro= IPR013818
SMART=
PROSITE = PDOC00110
SCOP = 1lpa
TCDB =
OPM family=
OPM protein= 1lpa
PDB=PDB3|1rp1 :18-353 PDB3|1lpaB:17-352 PDB3|1gpl :24-352PDB3|1n8sA:17-352 PDB3|1lpbB:17-352 PDB3|1ethC:1-336PDB3|1hplB:13-348 PDB3|1bu8A:17-353

Triglyceride lipases (EC number|3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester linkages of triglyceridescite journal |author=Chapus C, Rovery M, Sarda L, Verger R |title=Minireview on pancreatic lipase and colipase |journal=Biochimie |volume=70 |issue=9 |pages=1223–1234 |year=1988 |pmid=3147715 |doi=10.1016/0300-9084(88)90188-5] . Lipases are widely distributed in animals, plants and prokaryotes.

At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC number|3.1.1.34), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL)cite journal |author=Persson B, Bengtsson-Olivecrona G, Enerback S, Olivecrona T, Jornvall H |title=Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase |journal=Eur. J. Biochem. |volume=179 |issue=1 |pages=39–45 |year=1989 |pmid=2917565 |doi=10.1111/j.1432-1033.1989.tb14518.x] .

The most conserved region in all these proteins is centred around a serine residue which has been showncite journal |author=Blow D |title=Enzymology. More of the catalytic triad |journal=Nature |volume=343 |issue=6260 |pages=694–695 |year=1990 |pmid=2304545 |doi=10.1038/343694a0] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC number|2.3.1.43) (LCAT)cite journal |author=McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R |title=Cloning and expression of human lecithin-cholesterol acyltransferase cDNA |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue=8 |pages=2335–2339 |year=1986 |pmid=3458198 |doi=10.1073/pnas.83.8.2335] , which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Human proteins containing this domain

LIPC; LIPG; LIPH; LIPI; LPL; PLA1A; PNLIP; PNLIPRP1;
PNLIPRP2; PNLIPRP3;

References

Further reading

* [1] . Structure and activity of rat pancreatic lipase-related protein 2. Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M; J Biol Chem 1998;273:32121-32128. PMID|9822688