PMID:9562546
| Citation |
Huber-Wunderlich, M and Glockshuber, R (1998) A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3:161-71 |
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| Abstract |
Disulfide exchange reactions are catalyzed by thiol/disulfide oxidoreductases. These enzymes possess a thioredoxin fold and contain a catalytic disulfide with the sequence Cys-X-X-Cys at the N terminus of an alpha helix. Despite these similarities, the various members differ strongly in their redox potentials (-122 mV to -270 mV). Using the strong oxidant DsbA from Escherichia coli as a model system, we investigated whether the redox properties of these enzymes can be modulated rationally by exchange of the X-X dipeptide. |
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| Keywords |
Dipeptides; Enzyme Stability; Glutaredoxins; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Protein Disulfide-Isomerases/genetics; Protein Disulfide-Isomerases/metabolism; Proteins/metabolism; Substrate Specificity; Sulfur-Sulfur Bond Isomerases/genetics; Sulfur-Sulfur Bond Isomerases/metabolism; Thioredoxins/metabolism |
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