Aminopeptidase from Aeromonas proteolytica (AAP)

Aminopeptidase from Aeromonas proteolytica (AAP) is a prototypical bacterial metalloenzyme that catalyzes the sequential removal of N-terminal amino acids from peptides and proteins. It is notable for containing a dinuclear (two zinc ions) active site with equivalent roles in catalysis, making it a model system for studying co-catalytic mechanisms in metallohydrolases. AAP is a monomeric hydrolase of approximately 29.5 kDa, highly stable under a range of conditions, with broad substrate specificity for hydrophobic N-terminal residues. Its well-characterized structure and mechanism make it important for studies in enzymology, inhibitor design, and as a representative for understanding bacterial aminopeptidases, though it is not itself a direct human drug target.

Other names

Aeromonas proteolytica aminopeptidaseAAPAeromonas aminopeptidaseAeromonas proteolytica leucine aminopeptidase

Inhibitors act by chelating the catalytic zinc ions or by binding to the active site and blocking substrate access.