Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.2 | - |
L-aspartate | native enzyme | Escherichia coli | |
1.23 | - |
L-aspartate | tetrameric mutant enzyme maspase 3 | Escherichia coli | |
2.6 | - |
L-aspartate | dimeric mutant enzyme maspase 2 | Escherichia coli | |
5.5 | - |
L-aspartate | monomeric mutant enzyme maspase 1 | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | maximal activity: 1.0 mM for native enzyme, 2.2 mM for monomeric mutant enzyme maspase 1, 1.8 mM for dimeric mutant enzyme maspase 2, 1.6 mM for tetrameric mutant enzyme maspase 3 | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
56000 | - |
1 * 56000, mutant enzyme maspase 1, SDS-PAGE | Escherichia coli |
56000 | - |
2 * 56000, mutant enzyme maspase 2, SDS-PAGE | Escherichia coli |
56000 | - |
4 * 56000, mutant enzyme maspase 3, SDS-PAGE | Escherichia coli |
56200 | - |
monomeric mutant enzyme maspase 1, gel filtration | Escherichia coli |
109600 | - |
dimeric mutant enzyme maspase 2, gel filtration | Escherichia coli |
213800 | - |
tetrameric mutant enzyme maspase 3, gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
plasmid carrying the L-aspartase gene | - |
Escherichia coli J2 | - |
plasmid carrying the L-aspartase gene | - |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Escherichia coli | fumarate + NH3 | - |
? | |
L-aspartate | - |
Escherichia coli J2 | fumarate + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 56000, mutant enzyme maspase 2, SDS-PAGE | Escherichia coli |
monomer | 1 * 56000, mutant enzyme maspase 1, SDS-PAGE | Escherichia coli |
tetramer | 4 * 56000, mutant enzyme maspase 3, SDS-PAGE | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
maspase 1 | insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained | Escherichia coli |
maspase 2 | insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained | Escherichia coli |
maspase 3 | insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained | Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
30 min, native enzyme loses 83% of initial activity, monomeric mutant enzyme maspase 1 loses 23% of initial activity, dimeric mutant enzyme maspase 2 loses 48% of initial activity, tetrameric mutant enzyme maspase 3 loses 59% of initial activity | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
163 | - |
L-aspartate | monomeric mutant enzyme maspase 1 | Escherichia coli | |
165 | - |
L-aspartate | dimeric mutant enzyme maspase 2 | Escherichia coli | |
170 | - |
L-aspartate | tetrameric mutant enzyme maspase 3 | Escherichia coli | |
180 | - |
L-aspartate | native enzyme | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.3 | - |
monomeric mutant enzyme maspase 1 | Escherichia coli |
6.8 | - |
dimeric mutant enzyme maspase 2 | Escherichia coli |
7.1 | - |
tetrameric mutant enzyme maspase 3 | Escherichia coli |
7.5 | - |
native enzyme | Escherichia coli |