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Proteins/UNIPROT:Q86YB8
Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis..
Function from UniProtKB (Q86YB8), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
9 statements
9 statements · 3 reference databases · Subject: ERO1B · Sources: Hetionet, Reactome, UniProt
2 reactions
2CHEBI:16520+dioxygenCHEBI:17412+hydrogen peroxide
Catalysed by QSOX1 or GFER or QSOX2 or ERO1B or ERO1A
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:17357CC BY 4.0Reference data
[protein]-dithiol+dioxygen[protein]-disulfide+hydrogen peroxide
Catalysed by GFER or
5 names
Resolves to: ERO1B
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:59116CC BY 4.0Reference data