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 about 2.7fold 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 | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.88 | - |
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) | mutant G304K, pH 5.5, 25°C | Escherichia coli | |
3.79 | - |
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) | wild-type, pH 5.5, 25°C | 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. |
---|---|---|---|---|---|---|
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2 | - |
Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CueO | - |
Escherichia coli |
YacK | - |
Escherichia coli |