Pancreatic lipase family

Complex of human pancreatic lipase with colipase
Identifiers
Symbol Lipase
Pfam PF00151
InterPro IPR013818
PROSITE PDOC00110
SCOP 1lpa
SUPERFAMILY 1lpa
OPM protein 1lpa

Triglyceride lipases (EC 3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides.[1] 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 3.1.1.34), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL).[2]

The most conserved region in all these proteins is centred on a serine residue which has been shown[3] 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 2.3.1.43) (LCAT),[4] 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

  1. Chapus C, Rovery M, Sarda L, Verger R (1988). "Minireview on pancreatic lipase and colipase". Biochimie 70 (9): 1223–1234. doi:10.1016/0300-9084(88)90188-5. PMID 3147715.
  2. Persson B, Bengtsson-Olivecrona G, Enerback S, Olivecrona T, Jornvall H (1989). "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase". Eur. J. Biochem. 179 (1): 39–45. doi:10.1111/j.1432-1033.1989.tb14518.x. PMID 2917565.
  3. Blow D (1990). "Enzymology. More of the catalytic triad". Nature 343 (6260): 694–695. doi:10.1038/343694a0. PMID 2304545.
  4. McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R (1986). "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (8): 2335–2339. doi:10.1073/pnas.83.8.2335. PMC 323291. PMID 3458198.

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR013818


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