Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme is induced and activated by uterine decidualization | Mus musculus |
Application | Comment | Organism |
---|---|---|
biotechnology | enzyme might contribute to the remodeling of extracellular components after decidualization | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | secreted | Mus musculus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
polypeptide + H2O | Mus musculus | - |
peptides | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q61955 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys | enzyme is a trypsin-type serine protease | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
uterus | low activity in nonpregnant uteri, increased activity in pregnant uteri, highest at midgestational period | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
polypeptide + H2O | - |
Mus musculus | peptides | - |
? | |
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O | - |
Mus musculus | tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mus musculus |