EC Number   |
Cofactor |
Reference |
|---|
    1.4.3.21 | 2,4,5-trihydroxyphenylalanine quinone |
- |
391949, 655781, 724173, 724280, 724283, 724322, 724323, 724373, 724537, 724675, 725314, 725536, 725549, 725733, 726290, 726438, 726536, 741510 |
| 1.4.3.21 | 2,4,5-trihydroxyphenylalanine quinone |
enzyme contains one per monomer |
654501 |
| 1.4.3.21 | 2,4,5-trihydroxyphenylalanine quinone |
i.e. TPQ, covalently bound cofactor, one per monomer, generated by posttranslational modification of the first conserved tyrosine residue in the consensus sequence Asn-Tyr-(Glu/Asp)-Tyr |
703506 |
| 1.4.3.21 | 2,4,5-trihydroxyphenylalaninequinone |
i.e. TPQ cofactor |
701483, 701561 |
| 1.4.3.21 | 2,4,5-trihydroxyphenylalaninequinone |
i.e. TPQ cofactor, the cofactor is spontaneously formed by post-translational modifications of active site amino-acid residues |
701490 |
| 1.4.3.21 | FAD |
dependent on |
701487 |
| 1.4.3.21 | FAD |
flavoenzyme, a hydrophobic cavity extends from the protein surface to the active site, where a noncovalently bound FAD sits at the base of an aromatic cage, the sides of which are formed by Trp430 and Phe466, binding structure, overview |
705128 |
| 1.4.3.21 | L-topaquinone |
- |
742881 |
| 1.4.3.21 | L-topaquinone |
each subunit of the homodimer contains a protein-derived quinone cofactor, topaquinone. The reduced cofactor formed in the initial reductive half-reaction has two distinct conformations: a semiquinone radical form (TPQsq), in which the 4-hydroxyl group of the cofactor is ligated axially to the copper center, and an aminoresorcinol form (TPQamr), in which the cofactor has no direct contact with the copper. In crystallo thermodynamic analysis of the conformational change of the topaquinone cofactor in the copper amine oxidase |
765678 |
| 1.4.3.21 | more |
contains one "active-carbonyl" cofactor per dimer |
391914 |
