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

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

Publikováno v: International journal of molecular sciences (Online) 23 (2022): 1–14. doi:10.3390/ijms23010443
info:cnr-pdr/source/autori:Sandomenico, Annamaria; Gogliettino, Marta; Iaccarino, Emanuela; Fusco, Carmela; Caporale, Andrea; Ruvo, Menotti; Palmieri, Gianna; Cocca, Ennio/titolo:Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme/doi:10.3390%2Fijms23010443/rivista:International journal of molecular sciences (Online)/anno:2022/pagina_da:1/pagina_a:14/intervallo_pagine:1–14/volume:23
International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 443
International Journal of Molecular Sciences, Vol 23, Iss 443, p 443 (2022)
International Journal of Molecular Sciences

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 as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a7d4201328575f2d00d22ad27003907
http://www.cnr.it/prodotto/i/462624

Involvement of thioredoxin y2 in the preservation of leaf methionine sulfoxide reductase capacity and growth under high light

Autor: Laugier, Edith, Tarrago, Lionel, Courteille, Agathe, Innocenti, Gilles, Eymery, Françoise, Rumeau, Dominique, Issakidis-Bourguet, Emmanuelle, Rey, Pascal

Publikováno v: Plant, Cell and Environment
Plant, Cell and Environment, Wiley, 2013, 36 (3), pp.670-682. ⟨10.1111/pce.12005⟩
Plant, Cell and Environment, 2013, 36 (3), pp.670-682. ⟨10.1111/pce.12005⟩
Plant, Cell & Environment
Plant, Cell & Environment, 2013, 36 (3), pp.670-682. ⟨10.1111/pce.12005⟩

Methionine (Met) in proteins can be oxidized to two diastereoisomers of methionine sulfoxide, Met‐S‐O and Met‐R‐O, which are reduced back to Met by two types of methionine sulfoxide reductases (MSRs), A and B, respectively. MSRs are generally

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::42553566b77dbf39d9acf2f9c0b3e65d
https://hal.inrae.fr/hal-02929718

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