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Structural and Mechanistic Insights into Unusual Thiol Disulfide Oxidoreductase

Abstract : Background: TDOR are ubiquitous and catalyze important cell redox reactions. Results: Dtrx presents atypical physicochemical properties and a positive surface around its active site, suggesting a specificity for it(s) substrate(s). Conclusion: Active site histidine plays an important role in the molecular mechanism of Dtrx catalysis. Significance: Structural and functional studies of such atypical systems will give new insights into the TDOR catalytic mechanism.
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Submitted on : Wednesday, February 13, 2019 - 4:14:01 PM
Last modification on : Wednesday, October 27, 2021 - 10:00:07 AM
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J. Biol. Chem.-2012-Garcin-168...
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Edwige Garcin, Olivier Bornet, Latifa Elantak, Nicolas Vita, Laetitia Pieulle, et al.. Structural and Mechanistic Insights into Unusual Thiol Disulfide Oxidoreductase. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (3), pp.1688-1697. ⟨10.1074/jbc.m111.288316⟩. ⟨hal-02018153⟩

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