Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Dichek, H.L.; Parrott, C.; Ronan, R.; Brunzell, J.D.; Brewer, H.B.; Santamarina-Fojo, S.
    Functional characterization of a chimeric lipase genetically engineered from human lipoprotein lipase and human hepatic lipase (1993), J. Lipid Res., 34, 1393-1401.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3
-
Homo sapiens
3.1.1.34 chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 additional information chimeric lipase from lipoprotein lipase and hepatic lipase Homo sapiens
3.1.1.34 additional information chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase. The chimeric enzyme hydrolyzes both long chain and short chain fatty acid triacylglycerols and has catalytic properties that are similar to lipoprotein lipase Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Homo sapiens
-
chimeric lipase from lipoprotein lipase and hepatic lipase
-
3.1.1.34 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 tributyrin + H2O
-
Homo sapiens butyric acid + ?
-
?
3.1.1.34 triolein + H2O
-
Homo sapiens ?
-
?