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Literature summary for 1.10.3.2 extracted from

  • Komori, H.; Kataoka, K.; Tanaka, S.; Matsuda, N.; Higuchi, Y.; Sakurai, T.
    Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity (2016), Acta Crystallogr. Sect. F, 72, 558-563 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
acetate the oxidizing activity of CueO for ABTS is enhanced by the addition of up to 300 mM acetate ion, although it decreases at higher concentrations Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
the acetate-bound form of the type II copper is found in the X-ray structure of CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. When CueO is crystallized in citrate buffer, the OH(-)-bound form is present exclusively Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P36649 bifunctional copper oxidase and laccase, cf. EC 1.16.3.4
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Synonyms

Synonyms Comment Organism
CueO
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Escherichia coli
YacK
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Escherichia coli