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Literature summary for 3.4.24.33 extracted from

  • Ingrosso, D.; Fowler, A.V.; Bleibaum, J.; Clarke, S.
    Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins (1989), Biochem. Biophys. Res. Commun., 162, 1528-1534.
    View publication on PubMed
Search for more literature for 3.4.24.33

Organism

Organism UniProt Comment Textmining
Pseudomonas fragi
-
 mutant
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Erythrocyte carbonic anhydrase I + H2O i.e. EC 4.2.1.1, cleavage at 5 Asp- and 1 Glu-residues Pseudomonas fragi ?
-
 ?
Human erythrocyte D-aspartyl-L-isoaspartyl methyltransferase isozyme I + H2O i.e. EC 2.1.1.77, cleavage sites: N-terminal side of Asp and 5 out of 9 Glu-residues Pseudomonas fragi ?
-
 ?
additional information cleavage specificity Pseudomonas fragi ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pseudomonas fragi