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Literature summary for 1.4.3.21 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
Search for more literature for 1.4.3.21

Crystallization (Commentary)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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

Organism UniProt Comment Textmining
Arthrobacter globiformis P46881
-
-

Purification (Commentary)

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