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Literature summary extracted from

  • Lin, G.; Liao, W.C.; Chiou, S.Y.
    Quantitative structure-activity relationships for the pre-steady-state inhibition of cholesterol esterase by 4-nitrophenyl-N-substituted carbamates (2000), Bioorg. Med. Chem., 8, 2601-2607.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.13 4-nitrophenyl-N-allyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa
3.1.1.13 4-nitrophenyl-N-butyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa
3.1.1.13 4-nitrophenyl-N-chloroethyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa
3.1.1.13 4-nitrophenyl-N-hexyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa
3.1.1.13 4-nitrophenyl-N-methylphenyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa
3.1.1.13 4-nitrophenyl-N-octyl carbamate mechanism of inhibition by these pseudo-substrate inhibitors, via a 2-step reaction including the formation of a tetrahedral enzyme-inhibitor adduct and the formation of the carbamyl-enzyme, inhibition kinetics Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.13 additional information
-
 additional information kinetics Sus scrofa

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.13 steryl ester + H2O = sterol + fatty acid a group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts, reaction mechanism, catalytic triad consists of Ser194, His435, and Asp320 Sus scrofa
a

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.13 4-nitrophenyl butyrate + H2O
-
 Sus scrofa 4-nitrophenol + butyrate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.13 bile salt-activated lipase
-
 Sus scrofa
3.1.1.13 CEase
-
 Sus scrofa
3.1.1.13 cholesterol esterase
-
 Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.1.13 0.0026
-
 4-nitrophenyl-N-butyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa
3.1.1.13 0.0032
-
 4-nitrophenyl-N-hexyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa
3.1.1.13 0.0036
-
 4-nitrophenyl-N-octyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa
3.1.1.13 0.0038
-
 4-nitrophenyl-N-allyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa
3.1.1.13 0.0044
-
 4-nitrophenyl-N-methylphenyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa
3.1.1.13 0.0058
-
 4-nitrophenyl-N-chloroethyl carbamate pH 7.0, 25°C, pre-steady-state kinetic Sus scrofa