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Literature summary extracted from

  • Tsuzuki, W.; Ue, A.; Nagao, A.; Endo, M.; Abe, M.
    Inhibitory effect of lysophosphatidylcholine on pancreatic lipase-mediated hydrolysis in lipid emulsion (2004), Biochim. Biophys. Acta, 1684, 1-7.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 lysophosphatidylcholine increases Km and reduces Vmax of the enzyme with triaclyglyrol substrates, not with monoacylglycerols, the activity is completely restored by addition of taurodeoxycholine or phospholipid Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 additional information
-
 additional information kinetics in presence of lysophosphatidylcholine and of taurodeoxycholine Sus scrofa
3.1.1.3 0.36
-
 triolein pH 7.0, 37°C Sus scrofa
3.1.1.3 0.47
-
 tricaprin pH 7.0, 37°C Sus scrofa
3.1.1.3 0.86
-
 1-olein pH 7.0, 37°C Sus scrofa
3.1.1.3 1.17
-
 1-caprin pH 7.0, 37°C Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.3 commercial preparation highly purified pancreatic lipase Sus scrofa
-
3.1.1.3 pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 1-caprin + H2O
-
 Sus scrofa glycerol + caprate
-
 ?
3.1.1.3 1-olein + H2O
-
 Sus scrofa glycerol + oleate
-
 ?
3.1.1.3 tricaprin + H2O
-
 Sus scrofa dicaprin + caprate
-
 ?
3.1.1.3 triolein + H2O
-
 Sus scrofa diolein + oleate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 Pancreatic lipase
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 7
-
 assay at Sus scrofa