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Literature summary extracted from

  • Okajima, T.; Kishishita, S.; Chiu, Y.C.; Murakawa, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Kuroda, S.; Tanizawa, K.
    Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase (2005), Biochemistry, 44, 12041-12048.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.21 holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method Arthrobacter globiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.21 0.0025
-
2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme Arthrobacter globiformis
1.4.3.21 0.0025
-
2-Phenylethylamine pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis
1.4.3.21 0.0034
-
2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 Co2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
1.4.3.21 Cu2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
1.4.3.21 Ni2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ Arthrobacter globiformis
1.4.3.21 Zn2+ besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Arthrobacter globiformis P46881
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.21 recombinant enzyme expressed in Escherichia coli Arthrobacter globiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 2-phenylethylamine + H2O + O2
-
Arthrobacter globiformis 2-phenylethanal + NH3 + H2O2
-
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Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 AGAO
-
Arthrobacter globiformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.21 0.63
-
2-Phenylethylamine pH 6.8, 30°C, Ni-activated enzyme Arthrobacter globiformis
1.4.3.21 0.92
-
2-Phenylethylamine pH 6.8, 30°C, Co-activated enzyme Arthrobacter globiformis
1.4.3.21 75.7
-
2-Phenylethylamine pH 6.8, 30°C, Cu-activated enzyme Arthrobacter globiformis