Pancreatic lipase family

Complex of human pancreatic lipase with colipase
Identifiers
SymbolLipase
PfamPF00151
InterProIPR013818
PROSITEPDOC00110
SCOP21lpa / SCOPe / SUPFAM
OPM superfamily127
OPM protein1lpa
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 a 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.

  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. Bibcode:1990Natur.343..694B. doi:10.1038/343694a0. PMID 2304545. S2CID 4281247.
  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. Bibcode:1986PNAS...83.2335M. doi:10.1073/pnas.83.8.2335. PMC 323291. PMID 3458198.