Literature summary for 1.10.3.2 extracted from

Galli, I.; Musci, G.; Bonaccorsi Di Patti, M.
Sequential reconstitution of copper sites in the multicopper oxidase CueO (2004), J. Biol. Inorg. Chem., 9, 90-95 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.21	-	p-phenylenediamine	presence of 0.25 mM Cu2+, pH 5, 30°C	Escherichia coli
3.31	-	p-phenylenediamine	presence of 0.1 mM Cu2+, pH 5, 30°C	Escherichia coli
7.25	-	p-phenylenediamine	presence of 0.01 mM Cu2+, pH 5, 30°C	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	mechanism of copper incorporation in CueO is sequential, with type 1 copper being the first to be reconstituted, followed by type 2 and type 3 sites. The copper content of the purified protein is routinely 0.5-0.6 Cu atoms/protein molecule	Escherichia coli

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
purified by passage on Sepharose derivatized with chloroethylamine followed by chromatography on Phenyl-Sepharose	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
p-phenylenediamine + O2	-	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)