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Literature summary for 3.1.1.34 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.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
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
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LPL
-
Homo sapiens