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Literature summary for 1.4.3.21 extracted from

  • Pirrat, P.; Smith, M.A.; Pearson, A.R.; McPherson, M.J.; Phillips, S.E.
    Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway (2008), Acta Crystallogr. Sect. F, 64, 1105-1109.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme with xenon is used as a molecular oxygen binding-site probe, 8 mg/ml protein in 100 mM HEPES pH 7 and 1.2 M sodium citrate, vappour diffusion method, 18°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ type-2 copper centre, role in the catalytic mechanism, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P46883
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699 Escherichia coli ?
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?

Subunits

Subunits Comment Organism
More Escherichia coli copper amine oxidase possesses an extra N-terminal domain that lies close to one entrance to the beta-sandwich in the structurally conserved beta-sandwich structure Escherichia coli

Synonyms

Synonyms Comment Organism
Copper amine oxidase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
2,4,5-trihydroxyphenylalaninequinone i.e. TPQ cofactor Escherichia coli