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Literature summary for 3.1.1.32 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
Search for more literature for 3.1.1.32

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1192
-
 pH 8.0, 37°C Sus scrofa

Substrates and Products (Substrate)

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

Synonyms Comment Organism
PPL
-
 Sus scrofa

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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