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Literature summary extracted from

  • Stout, J.S.; Sutton, L.D.; Quinn, D.M.
    Acylenzyme mechanism and solvent isotope effects for cholesterol esterase-catalyzed hydrolysis of p-nitrophenyl butyrate (1985), Biochim. Biophys. Acta, 837, 6-12.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.13 ethanol
-
 Sus scrofa
3.1.1.13 ethanol
-
 Bos taurus
3.1.1.13 methanol
-
 Sus scrofa
3.1.1.13 methanol
-
 Bos taurus
3.1.1.13 n-butanol
-
 Sus scrofa
3.1.1.13 n-butanol
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.13 0.052
-
 p-nitrophenyl butyrate
-
 Bos taurus
3.1.1.13 0.073
-
 p-nitrophenyl butyrate
-
 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.13 Bos taurus
-
-
-
3.1.1.13 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.13 removal of trypsin impurities from commercial CEase by affinity absorption on LBTI-agarose Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.13 pancreas
-
 Sus scrofa
-
3.1.1.13 pancreas
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.13 p-nitrophenyl butyrate + H2O
-
 Sus scrofa p-nitrophenol + butanoic acid
-
 ?
3.1.1.13 p-nitrophenyl butyrate + H2O
-
 Bos taurus p-nitrophenol + butanoic acid
-
 ?