General Stability | Organism |
---|---|
the enzyme activity is completely stable in presence of detergents, overview | Balistes capriscus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Hg2+ | 57% inhibition at 5 mM | Balistes capriscus | |
additional information | the enzyme activity is completely stable in presence of detergents, overview. No inhibition by EDTA, 2-nercaptoethanol, pepstatin A, Ca2+, Ba2+, Zn2+, Cu2+, Mg2+, Mn2+, K+, and Na+ | Balistes capriscus | |
PMSF | 80% inhibition at 1 mM, complete at 5 mM | Balistes capriscus | |
Soybean trypsin inhibitor | complete inhibition at 1 mg/ml | Balistes capriscus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.068 | - |
Nalpha-benzoyl-DL-arginine 4-nitroanilide | pH 10.5, 25°C | Balistes capriscus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
23200 | - |
gel filtration and native PAGE | Balistes capriscus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Balistes capriscus | - |
- |
- |
Oxidation Stability | Organism |
---|---|
about 87% of its initial activity remains after 1 h at 40°C in the presence of 1% sodium perborate, about 80% in the presence of 1% H2O2 | Balistes capriscus |
Purification (Comment) | Organism |
---|---|
native enzyme 13.9fold to homogeneity by acetone precipitation, gel filtration, and anion exchange chromatography | Balistes capriscus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
intestine | - |
Balistes capriscus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
4.03 | - |
purified enzyme, pH 10.5, 25°C | Balistes capriscus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O | - |
Balistes capriscus | Nalpha-benzoyl-DL-arginine + 4-nitroaniline | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 23200, SDS-PAGE | Balistes capriscus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Balistes capriscus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | 65 | 80% of maximal activitx at 20°C, maximal activity at 40°C, 50% at 55°C, profile, overview | Balistes capriscus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 55 | purified enzyme, 50% activity remaining at 55°C, stable at 20-40°C | Balistes capriscus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.76 | - |
Nalpha-benzoyl-DL-arginine 4-nitroanilide | pH 10.5, 25°C | Balistes capriscus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10.5 | - |
a highly alkaline trypsin from the Grey trigger fish | Balistes capriscus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | 12 | activity at pH 9.0, pH 11.5, and pH 12.0 is 86.5%, 92.6% and 52.4% of maximal activity at pH 10.5, respectively, profile, overview | Balistes capriscus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3 | 13 | purified enzyme, completely stable at pH 7.0-12.0, profile, overview | Balistes capriscus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
40.6 | - |
Nalpha-benzoyl-DL-arginine 4-nitroanilide | pH 10.5, 25°C | Balistes capriscus |