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Literature summary for 3.4.11.10 extracted from

  • Prescott, J.M.; Wagner, F.W.; Holmquist, B.; Vallee, B.L.
    Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites (1985), Biochemistry, 24, 5350-5356.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Vibrio proteolyticus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity Vibrio proteolyticus
Cu2+ can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity Vibrio proteolyticus
Ni2+ can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity Vibrio proteolyticus
Zn2+ zinc can be replaced by other metals, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of metal ions, sequence of addition effects activity Vibrio proteolyticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Peptides + H2O Vibrio proteolyticus
-
?
-
?

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Peptides + H2O
-
Vibrio proteolyticus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Vibrio proteolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Vibrio proteolyticus