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Literature summary for 3.1.1.34 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
Search for more literature for 3.1.1.34

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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

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

Organism

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

Purification (Commentary)

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

Source Tissue

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

Subunits

Subunits Comment Organism
dimer
-
 Mus musculus
dimer
-
 Bos taurus

Synonyms

Synonyms Comment Organism
LPL
-
 Mus musculus
LPL
-
 Bos taurus

Temperature Optimum [°C]

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

General Information

General Information Comment Organism
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
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