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Literature summary extracted from

  • Griffon, N.; Budreck, E.C.; Long, C.J.; Broedl, U.C.; Marchadier, D.H.; Glick, J.M.; Rader, D.J.
    Substrate specificity of lipoprotein lipase and endothelial lipase: studies of lid chimeras (2006), J. Lipid Res., 47, 1803-1811.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 E250Q site-directed mutagenesis, the mutant shows reduced triacylglyceride lipase activity compared to the wild-type endothelial lipase Homo sapiens
3.1.1.3 G241R site-directed mutagenesis, the mutant shows reduced triacylglyceride lipase activity compared to the wild-type endothelial lipase Homo sapiens
3.1.1.3 additional information construction of an 245R insertion mutant showing increased triacylglyceride lipase activity compared to the wild-type endothelial lipase, exchange of lid regions of the endothelial lipase with the one of the lipoprotein lipase, EC 3.1.1.34, resulting in a substantial increase of 4.2fold in the ratio of triglyceride lipase activity to phospholipase activity compared with wild-type endothelial lipase, but did not fully confer the high degree of preference of lipoprotein lipase for triacylglyceride substrates, the replacement of the lipoprotein lipase lid by the endothelial lipase lid consistently generated a decrease in the ratio of triglyceride lipase activity to phospholipase activity to 32.7% of the ratio of wild-type lipoprotein lipase, overview, domains tructure of chimeric proteins, overview Homo sapiens
3.1.1.34 additional information exchanging lids between lipoprotein lipase and endothelial lipase only partially shifts the substrate specificity of the enzymes. Studies of a double chimera possessing both the lid and the C-terminal domain (C-domain) of endothelial lipase in the lipoprotein lipase backbone showed that the role of the lid in determining substrate specificity does not depend on the nature of the C-domain of the lipase Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.3 triacylglycerol + H2O Homo sapiens endothelial lipase plays a central role in plasma lipoprotein metabolism diacylglycerol + a carboxylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Homo sapiens
-
-
-
3.1.1.34 Homo sapiens
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 additional information
-
 activities of wild-type and mutant enzymes, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 triacylglycerol + H2O endothelial lipase plays a central role in plasma lipoprotein metabolism Homo sapiens diacylglycerol + a carboxylate
-
 ?
3.1.1.3 triacylglycerol + H2O the endothelial lipase is more active as a phospholipase than as a triacylglyceride lipase Homo sapiens diacylglycerol + a carboxylate
-
 ?
3.1.1.3 triolein + H2O
-
 Homo sapiens diolein + oleate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 endothelial lipase
-
 Homo sapiens
3.1.1.3 More the enzyme belongs to the triglyceride lipase gene subfamily Homo sapiens
3.1.1.3 triglyceride lipase
-
 Homo sapiens