EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.27 | Calcium | supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level | Staphylococcus pseudintermedius |
EC Number | General Stability | Organism |
---|---|---|
3.4.24.27 | enzyme is stable in presence of CaCl2 | Staphylococcus pseudintermedius |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.27 | 1,10-phenanthroline | 5 mM, complete inhibition | Staphylococcus pseudintermedius | |
3.4.24.27 | alpha2-Macroglobulin | - |
Staphylococcus pseudintermedius | |
3.4.24.27 | EDTA | 5 mM, complete inhibition | Staphylococcus pseudintermedius | |
3.4.24.27 | additional information | not inhibitory: human blood serpins alpha-1-antitrypsin and alpha-1-antichymotrypsin | Staphylococcus pseudintermedius |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.24.27 | extracellular | supplementation of growth medium by calcium induces expression. Regulation by calcium ions is at posttranscriptional level | Staphylococcus pseudintermedius | - |
- |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | 35000 | - |
x * 35000, SDS-PAGE, x * 55170, calculated | Staphylococcus pseudintermedius |
3.4.24.27 | 55170 | - |
x * 35000, SDS-PAGE, x * 55170, calculated | Staphylococcus pseudintermedius |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.27 | Staphylococcus pseudintermedius | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.24.27 | incubation of impure enzyme at 37°C causes proteolysis of impurities, whereas the protease remains active and uncleaved | Staphylococcus pseudintermedius |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.27 | alpha-1-antichymotrypsin + H2O | cleavage within the sequence LSA-LVE | Staphylococcus pseudintermedius | ? | - |
? | |
3.4.24.27 | alpha-1-antitrypsin + H2O | cleavage within the sequence AMF-LEA | Staphylococcus pseudintermedius | ? | - |
? | |
3.4.24.27 | azocasein + H2O | - |
Staphylococcus pseudintermedius | ? | - |
? | |
3.4.24.27 | Azocoll + H2O | - |
Staphylococcus pseudintermedius | ? | - |
? | |
3.4.24.27 | hide powder azure + H2O | - |
Staphylococcus pseudintermedius | ? | - |
? | |
3.4.24.27 | additional information | preferentially, peptide bonds preceding hydrophobic residues are hydrolyzed, such as I, L or F at P1' position. The enzyme less frequently also cleaves substrates with hydrophilic residues such as E, T or Q in the P1' position | Staphylococcus pseudintermedius | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.24.27 | ? | x * 35000, SDS-PAGE, x * 55170, calculated | Staphylococcus pseudintermedius |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.24.27 | 37 | - |
incubation of impure enzyme at 37°C causes proteolysis of impurities, whereas the protease remains active and uncleaved | Staphylococcus pseudintermedius |