EC Number | Cloned (Comment) | Organism |
---|---|---|
1.10.3.2 | DNA and amino acid sequence determination and analysis, expression in Escherichia coli | Cyathus bulleri |
1.10.3.2 | expression in Escherichia coli | Cyathus bulleri |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.10.3.2 | 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide | 200 mM, 80% inhibition | Cyathus bulleri | |
1.10.3.2 | DTT | 1 mM, complete inhibition | Cyathus bulleri | |
1.10.3.2 | EDTA | 1 mM, 67% inhibition | Cyathus bulleri | |
1.10.3.2 | kojic acid | 5 mM, complete inhibition | Cyathus bulleri | |
1.10.3.2 | L-cysteine | 0.1 mM, complete inhibition | Cyathus bulleri | |
1.10.3.2 | p-coumaric acid | 5 mM, 60% inhibition | Cyathus bulleri | |
1.10.3.2 | Sodium azide | 0.05 M, complete inhibition | Cyathus bulleri |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.10.3.2 | copper | the enzyme is denatured in the presence of a number of denaturing agents and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase | Cyathus bulleri | |
1.10.3.2 | Cu2+ | zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase | Cyathus bulleri | |
1.10.3.2 | Zn2+ | zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase | Cyathus bulleri |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.10.3.2 | Cyathus bulleri | - |
- |
- |
1.10.3.2 | Cyathus bulleri | A8W7J6 | - |
- |
1.10.3.2 | Cyathus bulleri 195062 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.10.3.2 | - |
Cyathus bulleri |
1.10.3.2 | recombinant enzyme 82fold from Escherichia coli | Cyathus bulleri |
EC Number | Renatured (Comment) | Organism |
---|---|---|
1.10.3.2 | the enzyme is denatured in the presence of a number of denaturing agents (EDTA, DTT and GdnHCl) and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity | Cyathus bulleri |
1.10.3.2 | unfolding of the purified laccase, chemical reagents like 1-100 mM EDTA, 50-200 mM DTT and 1-6 M guanidinium hydrochloride, 100% activity is regained with 1 mM copper at pH 8.0 or by 1 mM Zn2+ at pH 5.5 | Cyathus bulleri |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.10.3.2 | 4000 | - |
purified recombinant enzyme | Cyathus bulleri |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.10.3.2 | 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Cyathus bulleri | ? | - |
? | |
1.10.3.2 | 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Cyathus bulleri 195062 | ? | - |
? | |
1.10.3.2 | 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2 | - |
Cyathus bulleri | ? | - |
? | |
1.10.3.2 | 2-methylphenol + O2 | i.e. guaiacol | Cyathus bulleri | ? | - |
? | |
1.10.3.2 | 2-methylphenol + O2 | i.e. guaiacol | Cyathus bulleri 195062 | ? | - |
? | |
1.10.3.2 | guaiacol + O2 | - |
Cyathus bulleri | ? + H2O | - |
? |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.10.3.2 | 4 | - |
- |
Cyathus bulleri |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.10.3.2 | 2 | 6 | - |
Cyathus bulleri |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.10.3.2 | additional information | - |
additional information | inhibition kinetics | Cyathus bulleri |