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Literature summary extracted from

  • Saysell, C.G.; Tambyrajah, W.S.; Murray, J.M.; Phillips, S.V.; McPherson, M.J.; Knowles, P.F.
    Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue (2002), Biochem. J., 365, 809-816.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.21 D383E turnover-number of mutant enzyme is reduced up to 2000fold, depending on pH-value Escherichia coli
1.4.3.21 D383N catalytically inactive mutant enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.21 tranylcypromine fully reversible competitive onhibitor Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.21 0.00088
-
 beta-phenylethylamine pH 8.0, mutant enzyme D383E Escherichia coli
1.4.3.21 0.0012
-
 beta-phenylethylamine pH 7.0, wild-type enzyme Escherichia coli
1.4.3.21 0.0017
-
 beta-phenylethylamine pH 7.5, wild-type enzyme Escherichia coli
1.4.3.21 0.0017
-
 beta-phenylethylamine pH 6.5, wild-type enzyme Escherichia coli
1.4.3.21 0.0018
-
 beta-phenylethylamine pH 6.0, wild-type enzyme Escherichia coli
1.4.3.21 0.0023
-
 beta-phenylethylamine pH 8.0, wild-type enzyme Escherichia coli
1.4.3.21 0.0023
-
 beta-phenylethylamine pH 5.75, wild-type enzyme Escherichia coli
1.4.3.21 0.00247
-
 beta-phenylethylamine pH 7.0, mutant enzyme D383E Escherichia coli
1.4.3.21 0.0078
-
 beta-phenylethylamine pH 5.5, wild-type enzyme Escherichia coli
1.4.3.21 0.00962
-
 beta-phenylethylamine pH 6.0, mutant enzyme D383E Escherichia coli
1.4.3.21 0.028
-
 beta-phenylethylamine pH 5.5, mutant enzyme D383E Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 Cu2+ contains one Cu2+ per monomer Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.21 0.0038
-
 mutant enzyme D383E Escherichia coli
1.4.3.21 11
-
 wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 2-phenylethylamine + H2O + O2
-
 Escherichia coli 2-phenylethanal + NH3 + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 ECAO
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.21 0.00612
-
 beta-phenylethylamine pH 8.0, mutant enzyme D383E Escherichia coli
1.4.3.21 0.00937
-
 beta-phenylethylamine pH 7.0, mutant enzyme D383E Escherichia coli
1.4.3.21 0.01163
-
 beta-phenylethylamine pH 5.5, mutant enzyme D383E Escherichia coli
1.4.3.21 0.012
-
 beta-phenylethylamine pH 6.0, mutant enzyme D383E Escherichia coli
1.4.3.21 9.6
-
 beta-phenylethylamine pH 5.5, wild-type enzyme Escherichia coli
1.4.3.21 11.45
-
 beta-phenylethylamine pH 5.75, wild-type enzyme Escherichia coli
1.4.3.21 13.32
-
 beta-phenylethylamine pH 7.5, wild-type enzyme Escherichia coli
1.4.3.21 13.68
-
 beta-phenylethylamine pH 8.0, wild-type enzyme Escherichia coli
1.4.3.21 14.98
-
 beta-phenylethylamine pH 7.0, wild-type enzyme Escherichia coli
1.4.3.21 20.7
-
 beta-phenylethylamine pH 6.0, wild-type enzyme Escherichia coli
1.4.3.21 20.77
-
 beta-phenylethylamine pH 6.5, wild-type enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.21 2,4,5-trihydroxyphenylalanine quinone enzyme contains one per monomer Escherichia coli