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Literature summary for 3.4.11.9 extracted from

  • Chen, K.C.S.; Buchanan, T.M.
    Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase (1980), J. Biol. Chem., 255, 1704-1710.
    View publication on PubMed

General Stability

General Stability Organism
complete loss of activity after dialysis Neisseria gonorrhoeae

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ activates Neisseria gonorrhoeae
Co2+ metal ion required, Co2+ is the best activator Neisseria gonorrhoeae
Mn2+ activates Neisseria gonorrhoeae

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Pro + H2O
-
Neisseria gonorrhoeae Ala + Pro
-
?
Ala-Pro-Gly + H2O
-
Neisseria gonorrhoeae Ala + Pro-Gly
-
?
Gly-Pro + H2O
-
Neisseria gonorrhoeae Gly + Pro
-
?
Gly-Pro-Ala + H2O
-
Neisseria gonorrhoeae Gly + Pro-Ala
-
?
Gly-Pro-Gly-Gly + H2O
-
Neisseria gonorrhoeae Gly + Pro-Gly-Gly
-
?
Gly-Pro-Hyp + H2O
-
Neisseria gonorrhoeae Gly + Pro-Hyp
-
?
Leu-Pro + H2O
-
Neisseria gonorrhoeae Leu + Pro
-
?
Leu-Pro-Gly-Gly + H2O
-
Neisseria gonorrhoeae Leu + Pro-Gly-Gly
-
?
Met-Pro + H2O
-
Neisseria gonorrhoeae Met + Pro
-
?
additional information the enzyme releases only amino acid X from the NH2-termini of peptides with the general structure X-Pro-Y-Z Neisseria gonorrhoeae ?
-
?
Phe-Pro + H2O
-
Neisseria gonorrhoeae Phe + Pro
-
?
Pro-Pro + H2O
-
Neisseria gonorrhoeae Pro
-
?
Ser-Pro + H2O
-
Neisseria gonorrhoeae Ser + Pro
-
?
Val-Pro + H2O
-
Neisseria gonorrhoeae Val + Pro
-
?