Literature summary extracted from

Voss, C.V.; Davies, B.S.; Tat, S.; Gin, P.; Fong, L.G.; Pelletier, C.; Mottler, C.D.; Bensadoun, A.; Beigneux, A.P.; Young, S.G.
Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1 (2011), Proc. Natl. Acad. Sci. USA, 108, 7980-7984.

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.1.1.34	C418Y	the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin	Homo sapiens
3.1.1.34	E421K	the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin	Homo sapiens

Organism

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

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.1.1.34	capillary	GPIHBP1 shuttles lipoprotein lipase from subendothelial spaces to the capillary lumen	Homo sapiens	-
3.1.1.34	microvascular endothelial cell	-	Homo sapiens	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.1.1.34	triolein + H2O	-	Homo sapiens	oleate + diolein	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.1.1.34	LPL	-	Homo sapiens

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Release 2023.1 (January 2023)