ERAP2 Activators

ERAP2 Activators are a diverse group of chemical compounds that indirectly enhance the functional activity of ERAP2, a key enzyme in the antigen presentation pathway. These activators work primarily by modulating the enzyme's interaction with peptide substrates or altering the pool of peptides available for ERAP2-mediated trimming. Amino acids like L-Lysine play a critical role, serving as substrates that directly engage with ERAP2, thereby influencing its enzymatic activity.

Furthermore, compounds like Phosphoramidon and MG-132, which are inhibitors of metalloproteases and proteasomes respectively, contribute to ERAP2 activation by affecting the peptide pool. This modulation is crucial for the enzyme's role in generating peptides that fit MHC class I molecules for immune recognition. Additionally, Z-L-Leucine, by interacting with ERAP2, influences the enzyme's peptide trimming dynamics. Similarly, antibiotics such as Bacitracin and protease inhibitors like Aprotinin, Leupeptin, and E-64 indirectly enhance ERAP2 activity by influencing the overall protease balance and the intracellular peptide environment.