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Literature summary for 1.4.3.21 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
Search for more literature for 1.4.3.21

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
tranylcypromine fully reversible competitive onhibitor Escherichia coli

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ECAO
-
 Escherichia coli

Turnover Number [1/s]

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

Cofactor

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