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Literature summary for 3.1.1.3 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
Search for more literature for 3.1.1.3

Inhibitors

Inhibitors Comment Organism Structure
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]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Pancreatic lipase
-
 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
7
-
 assay at Sus scrofa