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2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
?
ethylamine + H2O + O2
acetaldehyde + NH3 + H2O2
-
-
-
?
histamine + H2O + O2
1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
-
-
?
tyramine + H2O + O2
4-hydroxyphenylethanal + NH3 + H2O2
quantum mechanical hydrogen tunneling can be enhanced by an enzyme protein scaffold including the catalytic base that directly mediates the hydrogen transfer
-
-
?
2-phenylethylamine + H2O + O2
phenylacetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
very poor substrate
-
-
?
tyramine + H2O + O2
(4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
preferred substrate
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
?
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
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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
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
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+
copper
-
copper
bound by three His ligands of the active-site
Cu2+
dependent on
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
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+
Cu2+
each subunit of the homodimer contains a Cu2+ ion
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
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+
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0.0019 - 0.0038
2-Phenylethylamine
0.0025
2-Phenylethylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.1
benzylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.0104
tyramine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.0019
2-Phenylethylamine
pH 6.8, 30°C, Co2+-substituted enzyme
0.0021
2-Phenylethylamine
pH 6.8, 30°C, mutant enzyme D298A
0.0025
2-Phenylethylamine
pH 6.8, 30°C, native copper protein
0.0025
2-Phenylethylamine
pH 6.8, 30°C, wild-type enzyme
0.0025
2-Phenylethylamine
pH 6.8, 30°C, Co-activated enzyme
0.0025
2-Phenylethylamine
pH 6.8, 30°C, Cu-activated enzyme
0.0034
2-Phenylethylamine
pH 6.8, 30°C, Ni-activated enzyme
0.0038
2-Phenylethylamine
pH 6.8, 30°C, Ni2+-substituted enzyme
0.0163
O2
pH 6.8, 30°C, Co2+-substituted enzyme
0.0183
O2
pH 6.8, 30°C, Ni2+-substituted enzyme
0.0208
O2
pH 6.8, 30°C, native copper protein
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0.00021 - 76
2-Phenylethylamine
44
2-Phenylethylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.24
benzylamine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
35
tyramine
-
in 50mM HEPES buffer, pH 6.8, at 15°C
0.00021
2-Phenylethylamine
pH 6.8, 30°C, mutant enzyme D298A
0.63
2-Phenylethylamine
pH 6.8, 30°C, Ni-activated enzyme
0.92
2-Phenylethylamine
pH 6.8, 30°C, Co-activated enzyme
1.3
2-Phenylethylamine
pH 6.8, 30°C, Ni2+-substituted enzyme
1.51
2-Phenylethylamine
pH 6.8, 30°C, Co2+-substituted enzyme
75.7
2-Phenylethylamine
pH 6.8, 30°C, native copper protein
75.7
2-Phenylethylamine
pH 6.8, 30°C, Cu-activated enzyme
76
2-Phenylethylamine
pH 6.8, 30°C, wild-type enzyme
1.13
O2
pH 6.8, 30°C, Ni2+-substituted enzyme
1.24
O2
pH 6.8, 30°C, Co2+-substituted enzyme
110
O2
pH 6.8, 30°C, native copper protein
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hanging-drop vapor diffusion method. Crystal structures of a series of Ru(II)-wire-enzyme complexes differing with respect to the length of the alkane linker
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method
microdialysis using 1.05 M potassium-sodium tartrate in 25 mM HEPES buffer, pH 6.8 containing 45% (v/v) glycerol
purified recombinant C-terminal StrepII-tagged enzyme in complex with inhibitors benzylhydrazine or tranylcypromine, vapour diffusion in hanging drop method, mixing of protein solution containing about 10 mg/ml protein in 50 mM HEPES, pH 7.0, with well solution containing 1.6 M ammonium sulfate and 150 mM sodium citrate pH 7.0. CuSO4, in a twofold molar excess, 2 weeks. The crystals are then transferred to a sitting drop well solution containing 30% v/v glycerol and 2 mM benzylhydrazine dihydrochloride or 0.4 mM tranylcypromine for 30 min, X-ray diffraction structure determination and analysis at 1.65-1.86 A resolution
the X-ray crystal structure of D298K at 1.7 A resolution
X-ray crystal structures of the Co2+ and Ni2+-enzyme are solved at 2.0-1.8 A resolution
complexed with benzylhydrazine, 4-hydroxybenzylhydrazine and phenylhydrazine, micro dialysis method, using 1.05 M potassium sodium tartrate in 25mM HEPES buffer, pH 6.8, at 16°C
-
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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
J. Am. Chem. Soc.
125
1041-1055
2003
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Murakawa, T.; Okajima, T.; Kuroda, S.; Nakamoto, T.; Taki, M.; Yamamoto, Y.; Hayashi, H.; Tanizawa, K.
Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction
Biochem. Biophys. Res. Commun.
342
414-423
2006
Arthrobacter globiformis (P46881)
brenda
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
Biochemistry
44
12041-12048
2005
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Chiu, Y.C.; Okajima, T.; Murakawa, T.; Uchida, M.; Taki, M.; Hirota, S.; Kim, M.; Yamaguchi, H.; Kawano, Y.; Kamiya, N.; Kuroda, S.; Hayashi, H.; Yamamoto, Y.; Tanizawa, K.
Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase
Biochemistry
45
4105-4120
2006
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Moore, R.H.; Spies, M.A.; Culpepper, M.B.; Murakawa, T.; Hirota, S.; Okajima, T.; Tanizawa, K.; Mure, M.
Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis
J. Am. Chem. Soc.
129
11524-11534
2007
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Langley, D.B.; Brown, D.E.; Cheruzel, L.E.; Contakes, S.M.; Duff, A.P.; Hilmer, K.M.; Dooley, D.M.; Gray, H.B.; Guss, J.M.; Freeman, H.C.
Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis
J. Am. Chem. Soc.
130
8069-8078
2008
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Langley, D.B.; Trambaiolo, D.M.; Duff, A.P.; Dooley, D.M.; Freeman, H.C.; Guss, J.M.
Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine
Acta Crystallogr. Sect. F
64
577-583
2008
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Murakawa, T.; Hayashi, H.; Taki, M.; Yamamoto, Y.; Kawano, Y.; Tanizawa, K.; Okajima, T.
Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors
J. Biochem.
151
167-178
2012
Arthrobacter globiformis
brenda
Murakawa, T.; Hamaguchi, A.; Nakanishi, S.; Kataoka, M.; Nakai, T.; Kawano, Y.; Yamaguchi, H.; Hayashi, H.; Tanizawa, K.; Okajima, T.
probing the catalytic mechanism of copper amine oxidase from Arthrobacter globiformis with halide ions
J. Biol. Chem.
290
23094-23109
2015
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda
Murakawa, T.; Baba, S.; Kawano, Y.; Hayashi, H.; Yano, T.; Kumasaka, T.; Yamamoto, M.; Tanizawa, K.; Okajima, T.
In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase
Proc. Natl. Acad. Sci. USA
116
135-140
2019
Arthrobacter globiformis (P46881), Arthrobacter globiformis
brenda