Catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. Can degrade the glycated RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) protein but not the native protein. May be involved in the elimination of glycated proteins (PubMed:12966075). Plays a homeostatic role in sustaining the cytoplasmic antioxidative system. May contribute to the elimination of the oxidized proteins in the cytoplasm (PubMed:22398639). Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. Strongly inhibited by the serine protease inhibitor diisopropyl fluorophosphate. Optimum pH is 7.0. Homotetramer. Plants silencing AARE show enhanced ion leakage after oxidative treatment. Belongs to the peptidase S9C family.