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Literature summary extracted from

  • Aloulou, A.; Frikha, F.; Noiriel, A.; Bou Ali, M.; Abousalham, A.
    Kinetic and structural characterization of triacylglycerol lipases possessing phospholipase A1 activity (2014), Biochim. Biophys. Acta, 1841, 581-587.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.32 V260A site-directed mutagenesis, the mutation affects the enzyme's substrate specificity Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.32 Ca2+ required Sus scrofa

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3
-
Homo sapiens
3.1.1.3
-
Sus scrofa
3.1.1.3
-
Equus caballus

Source Tissue

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
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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
-
?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.32 37
-
assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.32 8
-
assay at Sus scrofa

General Information

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