Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
structure of G304K mutant at 1.49 A resolution. The mutant shows dramatic conformational changes in methionine-rich helix and the relative regulatory loop. In the structure of Cu-soaked enzyme, the addition of Cu ions induces further conformational changes in the regulatory loop and methionine-rich helix as a result of the new Cu-binding sites on the enzyme's surface | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
G304K | mutant shows markedly increased the laccase activity. Movements of the regulatory loop combined with the changes of the methionine-rich region may uncover the T1 Cu site allowing greater access of the substrate. Cuprous oxidase activity of mutant G304K is about 20% of wild-type activity, while the Km value is about 4times lower | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.08 | - |
[Cu(I)(MeCN4)]PF6+ | mutant G304K, pH 5, 18°C | Escherichia coli | |
0.427 | - |
[Cu(I)(MeCN4)]PF6+ | wild-type, pH 5, 18°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P36649 | bifunctional copper oxidase and laccase, cf. EC 1.10.3.2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[Cu(I)(MeCN4)]PF6+ + 4 H+ + O2 | - |
Escherichia coli | ? + 2 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CueO | - |
Escherichia coli |
YacK | - |
Escherichia coli |