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Literature summary for 1.4.3.21 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)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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
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

Organism UniProt Comment Textmining
Arthrobacter globiformis P46881
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AGAO
-
Arthrobacter globiformis

Turnover Number [1/s]

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