Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, expression in Escherichia coli | Cyathus bulleri |
expression in Escherichia coli | Cyathus bulleri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide | 200 mM, 80% inhibition | Cyathus bulleri | |
DTT | 1 mM, complete inhibition | Cyathus bulleri | |
EDTA | 1 mM, 67% inhibition | Cyathus bulleri | |
kojic acid | 5 mM, complete inhibition | Cyathus bulleri | |
L-cysteine | 0.1 mM, complete inhibition | Cyathus bulleri | |
p-coumaric acid | 5 mM, 60% inhibition | Cyathus bulleri | |
Sodium azide | 0.05 M, complete inhibition | Cyathus bulleri |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | |
Cu2+ | zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase | Cyathus bulleri | |
Zn2+ | zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase | Cyathus bulleri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyathus bulleri | - |
- |
- |
Cyathus bulleri | A8W7J6 | - |
- |
Cyathus bulleri 195062 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Cyathus bulleri |
recombinant enzyme 82fold from Escherichia coli | Cyathus bulleri |
Renatured (Comment) | Organism |
---|---|
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 |
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 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
4000 | - |
purified recombinant enzyme | Cyathus bulleri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Cyathus bulleri | ? | - |
? | |
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2 | - |
Cyathus bulleri 195062 | ? | - |
? | |
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2 | - |
Cyathus bulleri | ? | - |
? | |
2-methylphenol + O2 | i.e. guaiacol | Cyathus bulleri | ? | - |
? | |
2-methylphenol + O2 | i.e. guaiacol | Cyathus bulleri 195062 | ? | - |
? | |
guaiacol + O2 | - |
Cyathus bulleri | ? + H2O | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4 | - |
- |
Cyathus bulleri |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
2 | 6 | - |
Cyathus bulleri |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics | Cyathus bulleri |