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Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity
The bacterial peroxiredoxin AhpC, a cysteine-dependent peroxidase, can be converted through a single amino acid insertion to a disulfide reductase, AhpC*, active in the glutathione and glutaredoxin pathway. Here we show that, whereas AhpC* is inactive as a peroxidase, other point mutants in AhpC can...
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| Hauptverfasser: | , , , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2008
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2239235/ https://ncbi.nlm.nih.gov/pubmed/18206967 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2007.11.029 |
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