Application | Comment | Organism |
---|---|---|
medicine | anticancer drug | Bacillus licheniformis |
General Stability | Organism |
---|---|
the enzyme is stable in the presence of more than 3 M guanidine hydrochloride. The enzyme activity decreases by approximately 40%, when the purified L-asparaginase is incubated with human serum and its components respectively under in vitro conditions for 48 h | Bacillus licheniformis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | strongest inhibition | Bacillus licheniformis | |
4-phenylbutanoic acid | more than 80% residual activity at 10 mM | Bacillus licheniformis | |
Bromoacetic acid | - |
Bacillus licheniformis | |
Ca2+ | - |
Bacillus licheniformis | |
Cd2+ | - |
Bacillus licheniformis | |
Co2+ | - |
Bacillus licheniformis | |
dithiothreitol | - |
Bacillus licheniformis | |
EDTA | 30% residual activity at 10 mM | Bacillus licheniformis | |
EGTA | - |
Bacillus licheniformis | |
Hg2+ | - |
Bacillus licheniformis | |
Lactate | about 70% inhibition at 10 mM | Bacillus licheniformis | |
Mn2+ | - |
Bacillus licheniformis | |
Ni2+ | - |
Bacillus licheniformis | |
oxylate | about 70% inhibition at 10 mM | Bacillus licheniformis | |
p-chloromercuribenzoic acid | - |
Bacillus licheniformis | |
phenylmethylsulfonyl fluoride | more than 80% residual activity at 10 mM | Bacillus licheniformis | |
pyruvate | about 70% inhibition at 10 mM | Bacillus licheniformis | |
Urea | 30% residual activity at 10 mM | Bacillus licheniformis | |
Zn2+ | - |
Bacillus licheniformis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.014 | - |
L-asparagine | in 50 mM Tris-HCl buffer (pH 8.6), at 37°C | Bacillus licheniformis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | activates at 100 mM | Bacillus licheniformis | |
Na+ | activates at 100 mM | Bacillus licheniformis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33700 | - |
4 * 33700, SDS-PAGE | Bacillus licheniformis |
134800 | - |
gel filtration | Bacillus licheniformis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-asparagine + H2O | Bacillus licheniformis | less than 10% activity compared to L-asparagine | D-aspartate + NH3 | - |
? | |
L-asparagine + H2O | Bacillus licheniformis | highly specific substrate | L-aspartate + NH3 | - |
? | |
L-glutamine + H2O | Bacillus licheniformis | less than 1% activity compared to L-asparagine | L-glutamate + NH3 | - |
? | |
additional information | Bacillus licheniformis | no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
acetone precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration | Bacillus licheniformis |
Storage Stability | Organism |
---|---|
-20°C, 50 mM Tris-HCl (pH 8.6), 30 days, almost no loss of activity | Bacillus licheniformis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-asparagine + H2O | less than 10% activity compared to L-asparagine | Bacillus licheniformis | D-aspartate + NH3 | - |
? | |
L-asparagine + H2O | highly specific substrate | Bacillus licheniformis | L-aspartate + NH3 | - |
? | |
L-glutamine + H2O | less than 1% activity compared to L-asparagine | Bacillus licheniformis | L-glutamate + NH3 | - |
? | |
additional information | no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine | Bacillus licheniformis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 33700, SDS-PAGE | Bacillus licheniformis |
Synonyms | Comment | Organism |
---|---|---|
L-ASNase | - |
Bacillus licheniformis |
L-asparaginase | - |
Bacillus licheniformis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Bacillus licheniformis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 50 | the enzyme is active at the temperature range of 30-50°C and shows a steep decent in activity above 60°C | Bacillus licheniformis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2680 | - |
L-asparagine | in 50 mM Tris-HCl buffer (pH 8.6), at 37°C | Bacillus licheniformis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
- |
Bacillus licheniformis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 10 | - |
Bacillus licheniformis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
7 | 9 | the enzyme is maximally stable at pH range of 7.0 to 9.0 over a period of 24 h | Bacillus licheniformis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Bacillus licheniformis | calculated from amino acid sequence | - |
5.5 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1503 | - |
L-asparagine | in 50 mM Tris-HCl buffer (pH 8.6), at 37°C | Bacillus licheniformis |