A zinc-containing enzyme.

Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. The enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase.

Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn²⁺ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at temperatures of 70 °C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase.

Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.

One unit will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0 at 25 °C.

Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.

Dissolves in water at 0.9-1.1 mg/mL concentration to form a clear, colorless solution.