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Literature summary for 1.4.3.21 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
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Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis P46881
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Arthrobacter globiformis

Subunits

Subunits Comment Organism
homodimer
-
 Arthrobacter globiformis

Synonyms

Synonyms Comment Organism
AGAO
-
 Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
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