Literature summary extracted from

Wong, H.; Davis, R.C.; Nikazy, J.; Seebart, K.E.; Schotz, M.C.
Domain exchange: characterization of a chimeric lipase of hepatic lipase and lipoprotein lipase (1991), Proc. Natl. Acad. Sci. USA, 88, 11290-11294.

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.1.1.3	additional information	chimeric lipase constructed of the N-terminal 329 residues of hepatic lipase and the C-terminal 136 residues of human lipoprotein lipase is a functional lipase and posseses characteristics from both parental enzymes	Rattus norvegicus
3.1.1.34	additional information	chimeric lipase constructed of the N-terminal 329 residues of rat hepatic lipase linked to the C-terminal 136 residues of human lipoprotein lipase. The chimera hydrolyzes both monodisperse short-chain (esterase) and emulsified long-chain (lipase) triacylglycerol substrates with catalytic and kinetic properties closely resembling those of native lipase	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.1.3	Rattus norvegicus	-	chimeric lipase constructed of the N-terminal 329 residues of hepatic lipase and the C-terminal 136 residues of human lipoprotein lipase	-
3.1.1.34	Homo sapiens	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.1.1.3	liver	-	Rattus norvegicus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.1.1.3	trioleoylglycerol + H2O	-	Rattus norvegicus	oleic acid + ?	-	?

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Release 2023.1 (January 2023)