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Sandomenico A, Gogliettino M, Iaccarino E, et al. Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme. Int J Mol Sci. 2021;23(1)doi: 10.3390/ijms23010443.
Sandomenico, A., Gogliettino, M., Iaccarino, E., Fusco, C., Caporale, A., Ruvo, M., Palmieri, G., & Cocca, E. (2021). Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme. International journal of molecular sciences, 23(1), . https://doi.org/10.3390/ijms23010443
Sandomenico, Annamaria, et al. "Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme." International journal of molecular sciences vol. 23,1 (2021). doi: https://doi.org/10.3390/ijms23010443
Sandomenico A, Gogliettino M, Iaccarino E, Fusco C, Caporale A, Ruvo M, Palmieri G, Cocca E. Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme. Int J Mol Sci. 2021 Dec 31;23(1). doi: 10.3390/ijms23010443. PMID: 35008880; PMCID: PMC8745263.
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Int J Mol Sci. 2021 Dec 31;23(1). doi: 10.3390/ijms23010443.

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

International journal of molecular sciences

Annamaria Sandomenico, Marta Gogliettino, Emanuela Iaccarino, Carmela Fusco, Andrea Caporale, Menotti Ruvo, Gianna Palmieri, Ennio Cocca

Affiliations

  1. Institute of Biostructure and Bioimaging, National Research Council (CNR-IBB), 80134 Napoli, Italy.
  2. Institute of Biosciences and BioResources, National Research Council (CNR-IBBR), 80131 Napoli, Italy.
  3. Department of Medicine and Health Sciences, University of Molise, 86100 Campobasso, Italy.

PMID: 35008880 PMCID: PMC8745263 DOI: 10.3390/ijms23010443

Abstract

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 actual mechanisms have yet to be elucidated. We show that a synthetic fragment of GDF11 spanning the region 48-64 acquires sensitivity to the endopeptidase activity of APEH only when the methionines are transformed into the corresponding sulphoxide derivatives. The data suggest that the presence of sulphoxide-modified methionines is an important prerequisite for the substrates to be processed by APEH and that the residue is crucial for switching the enzyme activity from exo- to endoprotease. The cleavage occurs on residues placed on the C-terminal side of Met(O), with an efficiency depending on the methionine adjacent residues, which thereby may play a crucial role in driving and modulating APEH endoprotease activity.

Keywords: APEH; endoproteolytic activity; oxidative stress; oxidized methionine; oxidized substrates

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