Triglyceride lipases (EC 22.214.171.124)  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 126.96.36.199) , 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  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 188.8.131.52) (LCAT) , which catalyzes fatty acid transfer between
phosphatidylcholine and cholesterol. We have built a pattern from that region.
Drosophila vitellogenins are also related to lipases , but they have
lost their active site serine.
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Persson B., Bengtsson-Olivecrona G., Enerback S., Olivecrona T., Jornvall H.
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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