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 | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | type-2 copper centre, role in the catalytic mechanism, overview | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P46883 | - |
- |
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 | ? | - |
? |
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 | Comment | Organism |
---|---|---|
Copper amine oxidase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
2,4,5-trihydroxyphenylalaninequinone | i.e. TPQ cofactor | Escherichia coli |