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Literature summary for 1.4.3.21 extracted from

  • Smith, M.A.; Pirrat, P.; Pearson, A.R.; Kurtis, C.R.; Trinh, C.H.; Gaule, T.G.; Knowles, P.F.; Phillips, S.E.; McPherson, M.J.
    Exploring the roles of the metal ions in Escherichia coli copper amine oxidase (2010), Biochemistry, 49, 1268-1280.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.21

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
EDTA treatment with EDTA reduces the activity of wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
 2-Phenylethylamine wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity Escherichia coli
Cu2+ the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal Escherichia coli
Mg2+ enzyme activity is stimulated by 3 mM Escherichia coli
Mn2+ enzyme activity is stimulated by 3 mM Escherichia coli
additional information not activated by Zn2+ Escherichia coli
Sr2+ enzyme activity is stimulated by 3 mM Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RCH2NH2 + H2O + O2 Escherichia coli
-
 RCHO + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P46883
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography, and gel filtration 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
-
 ?
RCH2NH2 + H2O + O2
-
 Escherichia coli RCHO + NH3 + H2O2
-
 ?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
Copper amine oxidase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
12.4
-
 2-Phenylethylamine wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
2,4,5-trihydroxyphenylalanine quinone
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10330
-
 2-Phenylethylamine wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C Escherichia coli