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Literature summary extracted from

  • Boehme, L.; Baer, J.W.; Hoffmann, T.; Manhart, S.; Ludwig, H.H.; Rosche, F.; Demuth, H.U.
    Isoaspartate residues dramatically influence substrate recognition and turnover by proteases (2008), Biol. Chem., 389, 1043-1053.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.19.1 additional information Sus scrofa catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Sus scrofa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 Asp-Ala-p-nitroanilide + H2O
-
 Sus scrofa ?
-
 ?
3.4.19.1 Asp-Pro-p-nitroanilide + H2O
-
 Sus scrofa ?
-
 ?
3.4.19.1 isoAsp-Ala-p-nitroanilide + H2O
-
 Sus scrofa ?
-
 ?
3.4.19.1 isoD/DAEFRHDSGYEVHHQKLVFFAEDVGSNKGA-NH2 + H2O
-
 Sus scrofa ?
-
 ?
3.4.19.1 additional information catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids Sus scrofa ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AARE
-
 Sus scrofa
3.4.19.1 acylamino acid-releasing enzyme
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.1 30
-
 activity assay Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.1 7.2
-
 activity assay Sus scrofa