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Literature summary for 3.4.21.19 extracted from

  • Houmard, J.; Drapeau, G.R.
    Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds (1972), Proc. Natl. Acad. Sci. USA, 69, 3506-3509.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Staphylococcus aureus
-
-

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-
Staphylococcus aureus V8
-
-
-

Substrates and Products (Substrate)

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 ?
-
?