GRAUSCHOPF, U and WINTHER, JR and KORBER, P and ZANDER, T and DALLINGER, P and BARDWELL, JCA (1995) WHY IS DSBA SUCH AN OXIDIZING DISULFIDE CATALYST. CELL, 83 (6). pp. 947-955. ISSN 0092-8674, 1097-4172
Full text not available from this repository.Abstract
DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pK(a) of a single residue, Cys-30. The pK(a) of Cys-80 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BOND FORMATION INVIVO; ESCHERICHIA-COLI; ISOMERASE DSBA; REDOX PROPERTIES; ACTIVE-SITE; IN-VIVO; THIOREDOXIN; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:37 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52160 |
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