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 |
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 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.34 | Homo sapiens | P06858 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.1.34 | recombinant wild-type and mutant enzymes by heparin affinity chromatography | Homo sapiens |
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 | - |
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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.1.34 | dimer | - |
Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.34 | LPL | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.34 | 37 | - |
assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.34 | 8 | - |
assay at | Homo sapiens |
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 |