Application | Comment | Organism |
---|---|---|
analysis | biosensor for asparagine using a thermostable recombinant asparaginase from Archaeoglobus fulgidus immobilized in front of an ammonium-selective electrode. The biosensor has a detection limit of 0.06 mM for L-asparagine. It shows high stability | Archaeoglobus fulgidus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli as a fusion protein with a polyhistidine tail | Archaeoglobus fulgidus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.005 | - |
L-asparagine | pH 9.2, 70°C, recombinant enzyme | Archaeoglobus fulgidus | |
0.08 | - |
L-asparagine | pH 9.2, 37°C, recombinant enzyme | Archaeoglobus fulgidus | |
0.2 | - |
L-glutamine | pH 9.2, 70°C, recombinant enzyme | Archaeoglobus fulgidus | |
0.35 | - |
L-glutamine | pH 9.2, 37°C, recombinant enzyme | Archaeoglobus fulgidus | |
1.2 | - |
D-asparagine | pH 9.2, 70°C, recombinant enzyme | Archaeoglobus fulgidus | |
1.8 | - |
D-asparagine | pH 9.2, 37°C, recombinant enzyme | Archaeoglobus fulgidus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
after heat treatment to denature most of the native Escherichia coli proteins, the enzyme is purified by an immobilized metal ion affinity chromatography method | Archaeoglobus fulgidus |
Storage Stability | Organism |
---|---|
22°C, pH 9.2, 4 months, the enzyme retains about 90% of enzyme activity | Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-asparagine + H2O | catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine | Archaeoglobus fulgidus | D-aspartate + NH3 | - |
? | |
L-asparagine + H2O | catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine | Archaeoglobus fulgidus | L-aspartate + NH3 | - |
? | |
L-glutamine + H2O | recombinant enzyme has 4fold higher activity for L-asparagine than for L-glutamine | Archaeoglobus fulgidus | L-glutamate + NH3 | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
5 min, stable | Archaeoglobus fulgidus |
85 | - |
5 min, 30% loss of activity | Archaeoglobus fulgidus |
95 | - |
5 min, 90% loss of activity | Archaeoglobus fulgidus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.2 | - |
- |
Archaeoglobus fulgidus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | 10 | pH 8.0: about 70% of maximal activity, pH 10.0: about 85% of maximal activity | Archaeoglobus fulgidus |