Literature summary for 1.10.3.2 extracted from

Cortes, L.; Wedd, A.G.; Xiao, Z.
The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli (2015), Metallomics, 7, 776-785 .

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Protein Variants

Protein Variants	Comment	Organism
D360M	mutation at sites Cu5	Escherichia coli
M355L/D360N	mutation at sites Cu5	Escherichia coli
M358S/M362S	mutation at sites Cu6	Escherichia coli
M358S/M362S/M364S/M368S	mutations at sites Cu6,7	Escherichia coli
M364S/M368S	mutation at sites Cu7	Escherichia coli

Organism

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CueO	-	Escherichia coli
YacK	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	the three copper sites play related but distinct roles in CueO oxidase activities. The internal Cu5 site is part of the essential electron transfer pathway connecting surface-exposed sites Cu6 and Cu7 to site T1. Both Cu6 and Cu7 are dominant substrate-docking-oxidation sites on the protein surface. The two surface-exposed sites Cu6 and Cu7 are the direct substrate-docking-oxidation sites for both oxidase functions and buried site Cu5 channels electrons from the oxidations to the Type 1 site of the multicopper oxidase machinery	Escherichia coli

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Release 2023.1 (January 2023)