Literature summary for 3.1.1.34 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
triolein + H2O	-	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)