Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme

• Published in: International journal of molecular sciences Vol. 23; no. 1; p. 443
• Main Authors: Sandomenico, Annamaria, Gogliettino, Marta, Iaccarino, Emanuela, Fusco, Carmela, Caporale, Andrea, Ruvo, Menotti, Palmieri, Gianna, Cocca, Ennio
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 31.12.2021; MDPI
• Subjects: Amino acids; APEH; Chromatography; Endopeptidases; endoproteolytic activity; Enzymatic activity; Enzyme activity; Enzymes; Humans; Methionine; Models, Molecular; Oligopeptidase; Oxidation; Oxidation-Reduction; Oxidative stress; oxidized methionine; oxidized substrates; Peptide Hydrolases - metabolism; Peptides; Peptides - metabolism; Physiology; Prolyl oligopeptidase; Proteins; Residues; Serine proteinase; Substrate Specificity; Sulfoxides; oxidized methionine; APEH; endoproteolytic activity; oxidative stress; oxidized substrates

APEH is a ubiquitous and cytosolic serine protease belonging to the prolyl oligopeptidase (POP) family, playing a critical role in the processes of degradation of proteins through both exo- and endopeptidase events. Endopeptidase activity has been associated with protein oxidation; however, the actu...