Triglyceride lipases (EC 3.1.1.3) [1] are lipolytic enzymes that hydrolyzes
the ester bond of triglycerides. Lipases are widely distributed in animals,
plants and prokaryotes. In higher vertebrates there are at least three tissue-specific isozymes: pancreatic, hepatic, and gastric/lingual. These three types
of lipases are closely related to each other as well as to lipoprotein lipase
(EC 3.1.1.34) [2], which hydrolyzes triglycerides of chylomicrons and very low
density lipoproteins (VLDL).
The most conserved region in all these proteins is centered around a serine
residue which has been shown [3] to participate, with an histidine and an
aspartic acid residue, to 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. We have built a pattern from that region.
Note:
Drosophila vitellogenins are also related to lipases [5], but they have
lost their active site serine.
Last update:
December 2004 / Pattern and text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
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.
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