EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.1.3 | expressed in Pichia pastoris | Homo sapiens |
3.1.1.3 | expressed in Pichia pastoris | Sus scrofa |
3.1.1.3 | expressed in Pichia pastoris | Equus caballus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.1.32 | V260A | site-directed mutagenesis, the mutation affects the enzyme's substrate specificity | Sus scrofa |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.1.32 | Ca2+ | required | Sus scrofa |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.1.3 | 48000 | - |
x * 48000, SDS-PAGE | Homo sapiens |
3.1.1.3 | 48000 | - |
x * 48000, SDS-PAGE | Sus scrofa |
3.1.1.3 | 48000 | - |
x * 48000, SDS-PAGE | Equus caballus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.3 | triacylglycerol + H2O | Homo sapiens | - |
diacylglycerol + a carboxylate | - |
? | |
3.1.1.3 | triacylglycerol + H2O | Sus scrofa | - |
diacylglycerol + a carboxylate | - |
? | |
3.1.1.3 | triacylglycerol + H2O | Equus caballus | - |
diacylglycerol + a carboxylate | - |
? | |
3.1.1.32 | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.3 | Equus caballus | - |
- |
- |
3.1.1.3 | Homo sapiens | - |
- |
- |
3.1.1.3 | Sus scrofa | - |
- |
- |
3.1.1.32 | Sus scrofa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.1.3 | - |
Homo sapiens |
3.1.1.3 | - |
Sus scrofa |
3.1.1.3 | - |
Equus caballus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.1.3 | pancreas | - |
Homo sapiens | - |
3.1.1.3 | pancreas | - |
Sus scrofa | - |
3.1.1.3 | pancreas | - |
Equus caballus | - |
3.1.1.32 | pancreas | - |
Sus scrofa | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.1.32 | 1192 | - |
pH 8.0, 37°C | Sus scrofa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.3 | L-alpha-phosphatidylcholine + H2O | - |
Homo sapiens | ? | - |
? | |
3.1.1.3 | L-alpha-phosphatidylcholine + H2O | - |
Sus scrofa | ? | - |
? | |
3.1.1.3 | L-alpha-phosphatidylcholine + H2O | - |
Equus caballus | ? | - |
? | |
3.1.1.3 | olive oil + H2O | - |
Homo sapiens | ? | - |
? | |
3.1.1.3 | olive oil + H2O | - |
Sus scrofa | ? | - |
? | |
3.1.1.3 | olive oil + H2O | - |
Equus caballus | ? | - |
? | |
3.1.1.3 | triacylglycerol + H2O | - |
Homo sapiens | diacylglycerol + a carboxylate | - |
? | |
3.1.1.3 | triacylglycerol + H2O | - |
Sus scrofa | diacylglycerol + a carboxylate | - |
? | |
3.1.1.3 | triacylglycerol + H2O | - |
Equus caballus | diacylglycerol + a carboxylate | - |
? | |
3.1.1.3 | tributyrin + H2O | - |
Homo sapiens | ? | - |
? | |
3.1.1.3 | tributyrin + H2O | - |
Sus scrofa | ? | - |
? | |
3.1.1.3 | tributyrin + H2O | - |
Equus caballus | ? | - |
? | |
3.1.1.32 | 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 | ? | - |
? | |
3.1.1.32 | 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 | ? | - |
? | |
3.1.1.32 | 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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.1.3 | ? | x * 48000, SDS-PAGE | Homo sapiens |
3.1.1.3 | ? | x * 48000, SDS-PAGE | Sus scrofa |
3.1.1.3 | ? | x * 48000, SDS-PAGE | Equus caballus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.3 | lipase | - |
Homo sapiens |
3.1.1.3 | lipase | - |
Sus scrofa |
3.1.1.3 | lipase | - |
Equus caballus |
3.1.1.3 | triacylglycerol acylhydrolase | - |
Homo sapiens |
3.1.1.3 | triacylglycerol acylhydrolase | - |
Sus scrofa |
3.1.1.3 | triacylglycerol acylhydrolase | - |
Equus caballus |
3.1.1.32 | PPL | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.32 | 37 | - |
assay at | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.32 | 8 | - |
assay at | Sus scrofa |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.1.32 | evolution | the enzyme is a member of the pancreatic lipase family | Sus scrofa |
3.1.1.32 | 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 |