| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1981736 | FEBS Open Bio | 2014 | 5 Pages |
•PDIL1;1 efficiently catalyzed both disulfide bond formation and disulfide bond reduction.•Two redox-active sites of PDIL1;1 were involved in disulfide reduction.•Disulfide reduction activity of PDIL1;1 increased with increasing GSH concentration.
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1, PDIL1;4, and PDIL2;3) and found that PDIL1;1 exhibited the highest catalytic activity for both disulfide bond formation and disulfide bond reduction. The activity of PDIL1;1-catalyzed disulfide bond reduction, in which two redox-active sites were involved, was enhanced by increasing the glutathione concentration. These results suggest that PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging.
