Cloned (Comment) | Organism |
---|---|
cloning of the gene encoding the enzyme and expression in Escherichia coli | Penicillium amagasakiense |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5.7 | - |
beta-D-glucose | native enzyme | Penicillium amagasakiense | |
6.2 | - |
beta-D-glucose | recombinant enzyme | Penicillium amagasakiense | |
6.3 | - |
beta-D-glucose | deglycosylated enzyme | Penicillium amagasakiense | |
8.3 | - |
2-deoxy-D-glucose | recombinant enzyme | Penicillium amagasakiense | |
106 | - |
D-mannose | recombinant enzyme | Penicillium amagasakiense | |
384 | - |
D-xylose | recombinant enzyme | Penicillium amagasakiense | |
952 | - |
D-galactose | recombinant enzyme | Penicillium amagasakiense |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
60000 | - |
2 * 60000, SDS-PAGE, recombinant enzyme | Penicillium amagasakiense |
120000 | - |
recombinant enzyme, native PAGE | Penicillium amagasakiense |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Penicillium amagasakiense | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
no glycoprotein | recombinant enzyme is nonglycosylated | Penicillium amagasakiense |
Purification (Comment) | Organism |
---|---|
of the reactivated recombinant enzyme, using mild acidification and anion-exchange chromatography on Q-Sepharose | Penicillium amagasakiense |
Renatured (Comment) | Organism |
---|---|
refolding after treatment with 8 M urea and 30 mM dithiothreitol and subsequent dilution in a buffer containing reduced glutathione, FAD and glycerol | Penicillium amagasakiense |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Penicillium amagasakiense |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-deoxy-D-glucose + O2 + H2O | recombinant enzyme | Penicillium amagasakiense | 2-deoxy-D-glucono-1,5-lactone + H2O2 | - |
? | |
beta-D-glucose + O2 + H2O | glucose is the primary substrate, recombinant enzyme | Penicillium amagasakiense | D-glucono-1,5-lactone + H2O2 | - |
? | |
D-galactose + O2 + H2O | recombinant enzyme | Penicillium amagasakiense | ? + H2O2 | - |
? | |
D-xylose + O2 + H2O | recombinant enzyme | Penicillium amagasakiense | ? | - |
? | |
mannose + O2 + H2O | recombinant enzyme | Penicillium amagasakiense | ? + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 60000, SDS-PAGE, recombinant enzyme | Penicillium amagasakiense |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
28 | 40 | recombinant enzyme | Penicillium amagasakiense |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1950 | - |
beta-D-glucose | deglycosylated enzyme | Penicillium amagasakiense | |
2000 | - |
beta-D-glucose | recombinant enzyme | Penicillium amagasakiense | |
2000 | - |
beta-D-glucose | native enzyme | Penicillium amagasakiense |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.2 | 6.2 | recombinant enzyme | Penicillium amagasakiense |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4.5 | 5.2 | recombinant enzyme, exhibits more than 80% of the maximum activity | Penicillium amagasakiense |
5 | 7 | recombinant enzyme, more than 90% of the residual activity retained after 72 h incubation at room temperature | Penicillium amagasakiense |
6.2 | 6.5 | recombinant enzyme, exhibits more than 80% of the maximum activity | Penicillium amagasakiense |
7 | - |
above, the recombinant enzyme is slightly less stable than native and deglycosylated enzyme | Penicillium amagasakiense |