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Literature summary extracted from

  • Yau, M.H.; Wang, Y.; Lam, K.S.; Zhang, J.; Wu, D.; Xu, A.
    A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization (2009), J. Biol. Chem., 284, 11942-11952.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.34 angiopoietin-like protein 3 i.e. Angptl3, human, commercial preparation of recombinant enzyme, inhibits LPL activity in vitro and in vivo, structural basis for inhibition, overview. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 46-57 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase Bos taurus
3.1.1.34 angiopoietin-like protein 3 i.e. Angptl3, human, commercial preparation of recombinant enzyme, inhibits LPL activity in vitro and in vivo, structural basis for inhibition, overview. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 46-57 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase Mus musculus
3.1.1.34 angiopoietin-like protein 4 i.e. Angptl4, human, recombinantly expressed in Escherichia coli. It inhibits LPL activity in vitro and in vivo. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 44-55 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase, involving amino acid residues His46, Gln50, and Gln53, by disrupting the enzyme dimerization, overview. Structural basis for inhibition, overview. Mutants H46A, Q50A, and Q53A are not active against the enzyme Bos taurus
3.1.1.34 angiopoietin-like protein 4 i.e. Angptl4, human, recombinantly expressed in Escherichia coli. It inhibits LPL activity in vitro and in vivo. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 44-55 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase, involving amino acid residues His46, Gln50, and Gln53, by disrupting the enzyme dimerization, overview. Structural basis for inhibition, overview. Mutants H46A, Q50A, and Q53A are not active against the enzyme Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.34 cell surface bound Mus musculus 9986
-
3.1.1.34 cell surface bound Bos taurus 9986
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.34 Bos taurus
-
-
-
3.1.1.34 Mus musculus
-
 C57BL/6J mice
-
3.1.1.34 Mus musculus C57/BL6J
-
 C57BL/6J mice
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.34 biotinylated enzyme by sucrose density gradient centrifugation and heparin affinity chromatography Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.34 3T3-L1 cell preadipocyte cell line Mus musculus
-
3.1.1.34 adipocyte
-
 Mus musculus
-
3.1.1.34 adipocyte
-
 Bos taurus
-
3.1.1.34 additional information LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes Mus musculus
-
3.1.1.34 additional information LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes Bos taurus
-
3.1.1.34 myocyte
-
 Mus musculus
-
3.1.1.34 myocyte
-
 Bos taurus
-

Subunits

EC Number Subunits Comment Organism
3.1.1.34 dimer
-
 Mus musculus
3.1.1.34 dimer
-
 Bos taurus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.34 LPL
-
 Mus musculus
3.1.1.34 LPL
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.34 30
-
 assay at Mus musculus
3.1.1.34 30
-
 assay at Bos taurus

General Information

EC Number General Information Comment Organism
3.1.1.34 physiological function lipoprotein lipase is a principal enzyme responsible for the clearance of chylomicrons and very low density lipoproteins from the bloodstream. The activity of LPL is tightly modulated by multiple mechanisms in a tissue-specific manner in response to nutritional changes Mus musculus
3.1.1.34 physiological function lipoprotein lipase is a principal enzyme responsible for the clearance of chylomicrons and very low density lipoproteins from the bloodstream. The activity of LPL is tightly modulated by multiple mechanisms in a tissue-specific manner in response to nutritional changes Bos taurus