Reactome | ERO1B oxidizes P4HB

ERO1B oxidizes P4HB

Stable Identifier

R-HSA-9817575

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

5/5

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ERO1B catalyzes the reduction of the disulfide bond in HC53,56-P4HB to form P4HB plus H2O2 (Gross et al. 2006; Mezghrani et al. 2001; Wang et al. 2011). Studies of knockout mutant mice are consistent with this role for ERO1B, while also suggesting that other oxidoreductases, not annotated here, could play a role in this process in vivo (Zito et al. 2010a b). See also the review of oxidative protein folding by Hudson et al. (2015).

Literature References

PubMed ID	Title	Journal	Year
16407158	Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p Bentzur, M, Gross, E, Thorpe, C, Sevier, CS, Kaiser, CA, Heldman, N, Vitu, E, Fass, D	Proc Natl Acad Sci U S A	2006
20308425	ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis Ron, D, Blais, J, Chin, KT, Zito, E, Harding, HP	J Cell Biol	2010
25091901	Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum Gannon, SA, Thorpe, C, Hudson, DA	Free Radic Biol Med	2015
11707400	Manipulation of oxidative protein folding and PDI redox state in mammalian cells Simmen, T, Fassio, A, Sitia, R, Mezghrani, A, Benham, A, Braakman, I	EMBO J	2001
21145486	Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin Ron, D, Yang, Y, Zito, E, Melo, EP, Wahlander, Å, Neubert, TA	Mol Cell	2010
21091435	The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation Zhu, L, Wang, L, Wang, CC	Biochem J	2011