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Literature summary for 3.1.1.13 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Sus scrofa
-
pancreas
-
Bos taurus
-

Substrates and Products (Substrate)

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