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Literature summary extracted from

  • 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 (2019), Proc. Natl. Acad. Sci. USA, 116, 135-140 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.21 Cu2+ each subunit of the homodimer contains a Cu2+ ion Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Arthrobacter globiformis P46881
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.21
-
 Arthrobacter globiformis

Subunits

EC Number Subunits Comment Organism
1.4.3.21 homodimer
-
 Arthrobacter globiformis

Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 AGAO
-
 Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
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 Arthrobacter globiformis