Pancreatic lipase family
Mammalian protein found in Homo sapiens / From Wikipedia, the free encyclopedia
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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.
Identifiers | |||||||||
---|---|---|---|---|---|---|---|---|---|
Symbol | Lipase | ||||||||
Pfam | PF00151 | ||||||||
InterPro | IPR013818 | ||||||||
PROSITE | PDOC00110 | ||||||||
SCOP2 | 1lpa / SCOPe / SUPFAM | ||||||||
OPM superfamily | 127 | ||||||||
OPM protein | 1lpa | ||||||||
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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.