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Literature summary extracted from

  • Junge, W.; Heymann, E.
    Characterization of the isoenzymes of pig-liver esterase. 2. Kinetic studies (1979), Eur. J. Biochem., 95, 519-525.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.1 acetonitrile activates isoenzyme I, no increase in activity with isoenzyme V Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 acetone above 0.5 M Sus scrofa
3.1.1.1 bis(4-nitrophenyl) phosphate 0.01 mM, 30 min, 89% loss of activity of isoenzyme V, 97% loss of activity of isoenzyme I Sus scrofa
3.1.1.1 NaF 1 mM, 30 min, 55% loss of activity of isoenzyme I, 2% loss of activity of isoenzyme V Sus scrofa
3.1.1.1 paraoxon 0.001 mM, 30 min, complete inhibition of isoenzyme V, 95% loss of activity of isoenzyme I Sus scrofa
3.1.1.1 physostigmine 0.01 mM, 3 min, no loss of activity of isoenzyme V, 95% loss of activity of isoenzyme I Sus scrofa
3.1.1.1 PMSF 0.01 mM, 30 min, 94% loss of activity of isoenzyme V, 27% loss of activity of isoenzyme I Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.1 0.04
-
 methyl octanoate isoenzyme V Sus scrofa
3.1.1.1 0.043
-
 4-nitrophenyl acetate isoenzyme V Sus scrofa
3.1.1.1 0.05
-
 phenyl acetate isoenzyme V Sus scrofa
3.1.1.1 0.22
-
 4-nitrophenyl acetate isoenzyme I Sus scrofa
3.1.1.1 0.4
-
 methyl octanoate isoenzyme I Sus scrofa
3.1.1.1 0.43
-
 phenyl acetate isoenzyme I Sus scrofa
3.1.1.1 0.6
-
 butanilicain isoenzyme V Sus scrofa
3.1.1.1 1.6
-
 butanilicain isoenzyme I Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Sus scrofa
-
 isoenzyme I and V
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.1 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O
-
 Sus scrofa 4-nitrophenol + acetate
-
 ?
3.1.1.1 acetanilide + H2O
-
 Sus scrofa acetate + aniline
-
 ?
3.1.1.1 butanilicain + H2O
-
 Sus scrofa ?
-
 ?
3.1.1.1 butanilicain + H2O i.e. N-butylglycyl-2-chloro-6-methylanilide Sus scrofa ?
-
 ?
3.1.1.1 butyrylthiocholine + H2O
-
 Sus scrofa butyric acid + thiocholine
-
 ?
3.1.1.1 estrone acetate + H2O
-
 Sus scrofa estrone + acetate
-
 ?
3.1.1.1 methyl butyrate + H2O
-
 Sus scrofa methanol + butyrate
-
 ?
3.1.1.1 methyl hexanoate + H2O
-
 Sus scrofa methanol + hexanoate
-
 ?
3.1.1.1 methyl octanoate + H2O
-
 Sus scrofa methanol + octanoate
-
 ?
3.1.1.1 N-ethylglycine xylidide + H2O
-
 Sus scrofa ?
-
 ?
3.1.1.1 phenyl acetate + H2O
-
 Sus scrofa phenol + acetate
-
 ?
3.1.1.1 tributyrylglycerol + H2O
-
 Sus scrofa butyrate + glycerol
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 6.5
-
 hydrolysis of methyl hexanoate, isoenzyme V Sus scrofa
3.1.1.1 8
-
 hydrolysis of methyl hexanoate, isoenzyme I Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 5.5 9 about 60% of maximal activity at pH 5.5 and at pH 9.0, hydrolysis of methyl hexanoate, isoenzyme V Sus scrofa
3.1.1.1 5.5 9.5 pH 5.5: about 45% of maximal activity, pH 9.5: about 80% of maximal activity, hydrolysis of methyl hexanoate, isoenzyme I Sus scrofa