GPX7,8 catalyze peroxidation of P4HB (PDI)

Stable Identifier
R-HSA-3341296
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
21215271 Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

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

J. Mol. Biol. 2011
23454490 Protein disulfide isomerase and glutathione are alternative substrates in the one Cys catalytic cycle of glutathione peroxidase 7

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

Biochim. Biophys. Acta 2013
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
peroxidase activity of ERO1L:GPX7,8 [endoplasmic reticulum lumen]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created