GPX7,8 catalyze peroxidation of P4HB (PDI)

Stable Identifier
Homo sapiens
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Glutathione peroxidase 7 (GPX7) and GPX8 are atypical glutathione peroxidases that catalyze the peroxidation of protein disulfide isomerases, such as PDI (P4HB) (Nguyen et al. 2011 and inferred from mouse in Bosello-Travain et al. 2013). GPX7 and GPX8 are each able to form heterodimers with the sulfhydryl oxidase ERO1alpha (ERO1L) in the endoplasmic reticulum lumen. It is hypothesized that GPX7 and GPX8 use hydrogen peroxide produced by ERO1L.

Literature References
PubMed ID Title Journal Year
23454490 Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7

Maiorino, M, Bosello-Travain, V, Negro, A, Ursini, F, Conrad, M, Quartesan, S, Toppo, S, Roveri, A, Rossetto, M, Cozza, G, Zaccarin, M

Biochim. Biophys. Acta 2013
21215271 Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

Saaranen, MJ, Salo, KE, Raykhel, IB, Nguyen, VD, Karala, AR, Alanen, HI, Lappi, AK, Wang, L, Wang, CC, Ruddock, LW

J. Mol. Biol. 2011
Catalyst Activity

peroxidase activity of ERO1L:GPX7,8 [endoplasmic reticulum lumen]

Orthologous Events
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