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Article

Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.

Molecular biology of the cell - 1 May 2006

Sevier Carolyn S, Kaiser Chris A

Abstract excerpt

The membrane-associated flavoprotein Ero1p promotes disulfide bond formation in the endoplasmic reticulum (ER) by selectively oxidizing the soluble oxidoreductase protein disulfide isomerase (Pdi1p), which in turn can directly oxidize secretory proteins. Two redox-active disulfide bonds are essential for Ero1p oxidase activity: Cys100-Cys105 and Cys352-Cys355. Genetic and structural data indicate a disulfide bond...

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Identifiers

PMID: 16495342
DOI: 10.1091/mbc.e05-05-0417
PMCID: PMC1446090

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.PMID 16495342Read ↗

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

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