Literature summary for 1.10.3.2 extracted from

Djoko, K.Y.; Chong, L.X.; Wedd, A.G.; Xiao, Z.
Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase (2010), J. Am. Chem. Soc., 132, 2005-2015 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the affinity of site T4 for CuII shows a KD of 0.0055 microM	Escherichia coli

Organism

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

Renatured (Commentary)

Renatured (Comment)	Organism
incubation of apo-CueO with excess CuSO4 (10 equiv) in Mops buffer (pH 7) in the presence of GSH (1 mM) at 4°C leads to incorporation of copper ions	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,6-dimethoxyphenol + H2O	-	Escherichia coli	?	-	?

General Information

General Information	Comment	Organism
physiological function	in order to act as a phenol oxidase, a T4 copper atom must be in place to mediate electron transfer between the buried T1 copper center and the organic substrates. The lability of this copper center restricts optimal phenol oxidase activity to the micro- to nanomolar concentration range for available Cuaq2+. This suggests that CueO cannot function as a phenol oxidase in vivo	Escherichia coli

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Release 2023.1 (January 2023)