Aminopeptidase P2 Inhibitors

Aminopeptidase P2 inhibitors represent a diverse group of chemicals that can affect the enzymatic activity of Aminopeptidase P2 indirectly. These inhibitors typically function by interfering with the metal ions that are crucial for the aminopeptidase's catalytic activity, binding to the active site of the enzyme, or mimicking the transition state of peptide hydrolysis. Since Aminopeptidase P2 is a metalloenzyme, compounds like Bestatin, Amastatin, Probestin, Phosphoramidon, Actinonin, Captopril, Tosedostat, and Aspergillomarasmine A can inhibit its activity by chelating the zinc ion essential for its function. This chelation process disrupts the normal operation of the enzyme's active site, thus preventing the cleavage of peptides.

Additionally, some of these inhibitors could also interact with the enzyme-substrate complex or the enzyme's active site in a way that prevents substrate binding. For instance, Bestatin and Amastatin are known to occupy the active site of aminopeptidases competitively, thereby blocking access to natural substrates. Compounds like Actinonin, which is an antibiotic, have a broad-spectrum ability to inhibit various aminopeptidases, suggesting that their structural characteristics allow them to fit within the active sites of these enzymes, including APP2. Synthetic inhibitors like Leuhistin, Boroleucine, PAQ-22, and BEL-7402 have been designed or discovered based on their ability to interact with the active sites of aminopeptidase.