EC Number   |
Protein Variants |
Reference |
|---|
   3.1.1.34 | 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 |
716787 |
| 3.1.1.34 | D204E |
homozygous missense mutation identified in a patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity |
663812 |
| 3.1.1.34 | D9N |
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease |
695054 |
| 3.1.1.34 | 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 |
716787 |
| 3.1.1.34 | K430A/R432A/K434A/K440A/K441A |
the mutant LPL has little or no ability to bind to GPIHBP1 on the surface of cells |
693158 |
| 3.1.1.34 | more |
chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase. The chimeric enzyme hydrolyzes both long chain and short chain fatty acid triacylglycerols and has catalytic properties that are similar to lipoprotein lipase |
80846 |
| 3.1.1.34 | more |
chimeric lipase constructed of the N-terminal 329 residues of rat hepatic lipase linked to the C-terminal 136 residues of human lipoprotein lipase. The chimera hydrolyzes both monodisperse short-chain (esterase) and emulsified long-chain (lipase) triacylglycerol substrates with catalytic and kinetic properties closely resembling those of native lipase |
80847 |
| 3.1.1.34 | more |
chimeric molecule between human lipoprotein lipase and rat hepatic lipase |
80845 |
| 3.1.1.34 | more |
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 |
749916 |
| 3.1.1.34 | more |
enzyme coated with both dextrin (D) and ionic surfactant (i) via lyophilization, LPL-D1, is prepared by freeze-drying a solution containing LPL (52% protein), dextrin (D), and surfactant at a 1:2:1 weight ratio in 1:1 (v/v) water-dioxane. LPL-D1 is as active as its native counterpart in water but about 3000fold more active than the latter in organic solvent |
749450 |
