Endoplasmic reticulum oxidoreductase 1 beta (ERO1B)

Endoplasmic reticulum oxidoreductase 1 beta (ERO1B) is an endoplasmic reticulum-resident oxidoreductase enzyme that catalyzes the formation of protein disulfide bonds, particularly in the folding of nascent polypeptides. ERO1B efficiently reoxidizes protein disulfide isomerase (PDI), enabling continuous rounds of disulfide bond formation essential for proper protein folding. The enzyme uses flavin adenine dinucleotide (FAD) as a cofactor to relay electrons from PDI to molecular oxygen, thus producing hydrogen peroxide (H~2~O~2~) as a byproduct, which may contribute to intracellular reactive oxygen species generation. ERO1B is selectively and highly expressed in pancreatic and stomach tissues, where it is implicated in insulin biogenesis and glucose regulation. Dysregulation or overexpression of ERO1B and its paralog ERO1A are linked to diseases such as diabetes and cancer due to their roles in protein folding stress, cell migration, and apoptosis. The activity of ERO1B is tightly regulated to maintain cellular homeostasis and avoid harmful accumulation of oxidative species.

Other names

ERO1-like protein betaERO1LBERO1-L-betaERO1-L(beta)Ero1betaEndoplasmic reticulum oxidoreductase betaEndoplasmic reticulum oxidoreductin-1-like protein BOxidoreductin-1-L-beta

Inhibition of oxidative protein folding by blocking electron transfer from ERO1B to molecular oxygen; Targeting interaction with protein disulfide isomerase (PDI) to disrupt disulfide bond formation.