Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Staphylococcus aureus | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Staphylococcus aureus V8 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
insulin + H2O | A-chain and B-chain | Staphylococcus aureus | ? | - |
? | |
insulin + H2O | A-chain and B-chain | Staphylococcus aureus V8 | ? | - |
? | |
Lysozyme + H2O | - |
Staphylococcus aureus | ? | - |
? | |
Lysozyme + H2O | - |
Staphylococcus aureus V8 | ? | - |
? | |
additional information | cleaves specifically the peptide bonds on the carboxyl-terminal side of either Asp or Glu residues in phosphate buffer - pH 7.8, hydrolyzes only glutamoyl bonds - in either ammonium bicarbonate at pH 7.8 or ammonium acetate at pH 4.0. - of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The enzyme hydrolyzes all of the 16 different glutamoyl bonds studied, although those involving hydrophobic amino acid residues with bulky side chains are cleaved at a lower rate | Staphylococcus aureus | ? | - |
? | |
additional information | cleaves specifically the peptide bonds on the carboxyl-terminal side of either Asp or Glu residues in phosphate buffer - pH 7.8, hydrolyzes only glutamoyl bonds - in either ammonium bicarbonate at pH 7.8 or ammonium acetate at pH 4.0. - of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The enzyme hydrolyzes all of the 16 different glutamoyl bonds studied, although those involving hydrophobic amino acid residues with bulky side chains are cleaved at a lower rate | Staphylococcus aureus V8 | ? | - |
? | |
Ribonuclease + H2O | - |
Staphylococcus aureus | ? | - |
? | |
Ribonuclease + H2O | - |
Staphylococcus aureus V8 | ? | - |
? |