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PMID:9013867
| Citation |
Majoul, I, Ferrari, D and Söling, HD (1997) Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum. FEBS Lett. 401:104-8 |
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| Abstract |
Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-A2 by reduction of a disulfide bridge [Majoul et al. (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER favors disulfide formation. We show here that the disulfide bridge of CTX-A is cleaved in vitro already at GSH/GSSG ratios between 1 and 3. Protein disulfide isomerase (PDI) exerts only a minor accelerating effect. Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction. These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously. |
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| Keywords |
Animals; Binding Sites; Cercopithecus aethiops; Cholera Toxin/chemistry; Cholera Toxin/metabolism; Disulfides/chemistry; Disulfides/metabolism; Endoplasmic Reticulum/metabolism; Oxidation-Reduction; Vero Cells |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0015036: disulfide oxidoreductase activity |
ECO:0000314: |
F |
Figure 6 (lane 2 and 3). CTA get reduced in the presence of PDI (lane 3). Lane 2 is without PDI. |
complete | ||||
See also
References
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