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Literature summary extracted from

  • Hayne, C.K.; Lafferty, M.J.; Eglinger, B.J.; Kane, J.P.; Neher, S.B.
    Biochemical analysis of the lipoprotein lipase truncation variant, LPLS447X, reveals increased lipoprotein uptake (2017), Biochemistry, 56, 525-533 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.34 apoC-II derived from chylomicrons of a patient with severe hypertriglyceridemia, activates wild-type and enzyme mutant LPLS447X Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.34 additional information construction of the lipoprotein lipase truncation variant, LPLS447X, the truncation leads to increased lipoprotein uptake of the cells, gain-of-function phenotype in vivo. Mutant LPLS447X enhances lipoprotein uptake to a greater degree than wild-type LPL does Homo sapiens
3.1.1.34 S447X site-directed mutagenesis, the mutant is inhibited by angiopoietin-like protein 4 in the same way as the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.34 angiopoietin-like protein 4 ANGPTL4, ANGPTL4 inhibits LPL by a noncompetitive mechanism, unaltered in the presence or absence of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), inhibits wild-type and mutant LPLS447X enzymes to the same extent Homo sapiens
3.1.1.34 apoC-III derived from chylomicrons of a patient with severe hypertriglyceridemia, inhibits wild-type and enzyme mutant LPLS447X Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.34 additional information
-
 additional information Michaelis-Menten kinetics Homo sapiens
3.1.1.34 4.74
-
 triacylglycerol from chylomicrons, pH 8.0, 37°C, mutant LPLS447X Homo sapiens
3.1.1.34 6.09
-
 triacylglycerol from chylomicrons, pH 8.0, 37°C, wild-type enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.34 triacylglycerol + H2O Homo sapiens
-
 diacylglycerol + a carboxylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.34 Homo sapiens P06858
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.34 recombinant wild-type and mutant enzymes by heparin affinity chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.34 Huh-7 cell
-
 Homo sapiens
-
3.1.1.34 additional information GPIHBP1 is the protein responsible for translocation of enzyme LPL to the capillary lumen Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.34 1,2-di-O-lauryl-rac-glycero-3-(glutaric acid 6-methylresorufin ester) + H2O DGGR, a synthetic substrate that produces a fluorescent signal upon hydrolysis Homo sapiens ?
-
 ?
3.1.1.34 triacylglycerol + H2O
-
 Homo sapiens diacylglycerol + a carboxylate
-
 ?
3.1.1.34 triacylglycerol + H2O from chylomicrons, lipoproteins isolated from human blood Homo sapiens diacylglycerol + a carboxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.34 dimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.1.34 LPL
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.34 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.34 8
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
3.1.1.34 additional information the enzyme interacts with glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) and lipoprotein receptor-related protein (LRP), enzyme ligand interaction analysis by surface plasmon resonance. Enzyme structure modeling Homo sapiens
3.1.1.34 physiological function LPL is responsible for bridging the uptake of LDL and VLDL particles by the liver through an interaction mediated by the C-terminus of LPL. Angiopoietin-like protein 4 (ANGPTL4) and apolipoproteins regulate LPL, ANGPTL4 inhibits LPL by a noncompetitive mechanism Homo sapiens