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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P36649 | bifunctional copper oxidase and laccase, cf. EC 1.16.3.4 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,6-dimethoxyphenol + H2O | - |
Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CueO | - |
Escherichia coli |
YacK | - |
Escherichia coli |
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 |