Protein Variants | Comment | Organism |
---|---|---|
V260A | site-directed mutagenesis, the mutation affects the enzyme's substrate specificity | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Sus scrofa | the enzyme is a triacylglycerol lipase, EC 3.1.1.3, that is a carboxylester hydrolases catalyzing the hydrolysis of long-chain acylglycerols, but it is also active on phosphatidylcholine to a lesser extent | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
pancreas | - |
Sus scrofa | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1192 | - |
pH 8.0, 37°C | Sus scrofa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is a triacylglycerol lipase, EC 3.1.1.3, that is a carboxylester hydrolases catalyzing the hydrolysis of long-chain acylglycerols, but it is also active on phosphatidylcholine to a lesser extent | Sus scrofa | ? | - |
? | |
additional information | Val260 residue in enzyme's lid is critical for the interaction with lipid substrate, molecular dynamics calculations of lipase-phospholipid transition-state complexes in substrate binding determining the substrate specificity with phospholipids, molecular dynamics simulations, overview. Hydrolysis of egg yolk phosphatidylcholine by the enzyme shows a triphasic kinetic pattern | Sus scrofa | ? | - |
? | |
phosphatidylcholine + H2O | substrate from egg yolk, the regiospecificity and hydrolysis profile of the enzyme is typical of a PLA1 enzyme generating lysophosphatidic acid, but not hydrolyzing the ester bond at the sn-2 position | Sus scrofa | 2-acylglycerophosphocholine + a carboxylate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PPL | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Sus scrofa |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the pancreatic lipase family | Sus scrofa |
physiological function | classical pancreatic lipase may fulfill in some cases additional biological functions as a phospholipase A1, PLA1, enzyme, compensating pancreatic lipase-related protein 2, PLRP2, deficiency in the digestive tract | Sus scrofa |