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Literature summary extracted from

  • Kishishita, S.; Okajima, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Suzuki, S.; Kuroda, S.; Tanizawa, K.; Mure, M.
    Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes (2003), J. Am. Chem. Soc., 125, 1041-1055.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.21 X-ray crystal structures of the Co2+ and Ni2+-enzyme are solved at 2.0-1.8 A resolution Arthrobacter globiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.21 0.0019
-
 2-Phenylethylamine pH 6.8, 30°C, Co2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 0.0025
-
 2-Phenylethylamine pH 6.8, 30°C, native copper protein Arthrobacter globiformis
1.4.3.21 0.0038
-
 2-Phenylethylamine pH 6.8, 30°C, Ni2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 0.0163
-
 O2 pH 6.8, 30°C, Co2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 0.0183
-
 O2 pH 6.8, 30°C, Ni2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 0.0208
-
 O2 pH 6.8, 30°C, native copper protein Arthrobacter globiformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 Co2+ enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable Arthrobacter globiformis
1.4.3.21 Cu2+ copper protein. The native Cu2+ has essential roles such as catalyzing the electron transfer between the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen, in part by providing a binding site for 1e- and 2e- reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen Arthrobacter globiformis
1.4.3.21 Ni2+ enzyme reconstituted with Co2+ exhibits 0.9% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable 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
-
 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
-
 ?

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 1.13
-
 O2 pH 6.8, 30°C, Ni2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 1.24
-
 O2 pH 6.8, 30°C, Co2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 1.3
-
 2-Phenylethylamine pH 6.8, 30°C, Ni2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 1.51
-
 2-Phenylethylamine pH 6.8, 30°C, Co2+-substituted enzyme Arthrobacter globiformis
1.4.3.21 75.7
-
 2-Phenylethylamine pH 6.8, 30°C, native copper protein Arthrobacter globiformis
1.4.3.21 110
-
 O2 pH 6.8, 30°C, native copper protein Arthrobacter globiformis