| |  Online-Ressource |
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| Verfasst von: | Staudacher, Verena [VerfasserIn]  |
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| | Djuika, Carine F. [VerfasserIn] |
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| | Koduka, Joshua [VerfasserIn] |
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| | Schlossarek, Sarah [VerfasserIn] |
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| | Kopp, Jürgen [VerfasserIn] |
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| | Büchler-Schäff, Marleen [VerfasserIn] |
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| | Lanzer, Michael [VerfasserIn] |
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| | Deponte, Marcel [VerfasserIn] |
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| Titel: | Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins |
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| Verf.angabe: | Verena Staudacher, Carine F. Djuika, Joshua Koduka, Sarah Schlossarek, Jürgen Kopp, Marleen Büchler, Michael Lanzer, Marcel Deponte |
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| E-Jahr: | 2015 |
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| Jahr: | 5 May 2015 |
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| Umfang: | 9 S. |
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| Teil: | volume:85 |
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| | year:2015 |
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| | pages:228-236 |
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| | extent:9 |
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| Fussnoten: | Gesehen am 22.06.2020 |
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| Titel Quelle: | Enthalten in: Free radical biology and medicine |
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| Ort Quelle: | New York, NY [u.a.] : Elsevier, 1987 |
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| Jahr Quelle: | 2015 |
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| Band/Heft Quelle: | 85(2015), Seite 228-236 |
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| ISSN Quelle: | 1873-4596 |
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| Abstract: | Life under aerobic conditions has shaped peroxiredoxins (Prx) as ubiquitous thiol-dependent hydroperoxidases and redox sensors. Structural features that balance the catalytically active or inactive redox states of Prx, and, therefore, their hydroperoxidase or sensor function, have so far been analyzed predominantly for Prx1-type enzymes. Here we identify and characterize two modulatory residues of the Prx5-type model enzyme PfAOP from the malaria parasite Plasmodium falciparum. Gain- and loss-of-function mutants reveal a correlation between the enzyme parameters and the inactivation susceptibility of PfAOP with the size of residue 109 and the presence or absence of a catalytically relevant but nonessential cysteine residue. Based on our kinetic data and the crystal structure of PfAOPL109M, we suggest a novel mechanism for balancing the hydroperoxidase activity and inactivation susceptibility of Prx5-type enzymes. Our study provides unexpected insights into Prx structure-function relationships and contributes to our understanding of what makes Prx good enzymes or redox sensors. |
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| DOI: | doi:10.1016/j.freeradbiomed.2015.04.030 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.freeradbiomed.2015.04.030 |
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| | Volltext: http://www.sciencedirect.com/science/article/pii/S0891584915001938 |
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| | DOI: https://doi.org/10.1016/j.freeradbiomed.2015.04.030 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | Catalytic mechanism |
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| | Inactivation |
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| | Molecular evolution |
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| | Peroxiredoxin |
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| | Redox regulation |
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| K10plus-PPN: | 1701722747 |
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| Verknüpfungen: | → Zeitschrift |
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Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins / Staudacher, Verena [VerfasserIn]; 5 May 2015 (Online-Ressource)
