Regeneration of cytosolic thiol peroxidases

Three soluble type two peroxiredoxins (PRXIIB, C, D) and two glutathione peroxidase‐like enzymes (GPXL2, 8) reside in the cytosol of Arabidopsis thaliana cells and function both as thiol‐dependent antioxidants and redox sensors. Their primary substrate is H2O2, but they also accept other peroxides w...

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Bibliographic Details
Published in:Physiologia plantarum 2023-09, Vol.175 (5), p.e14042-n/a
Main Authors: Vogelsang, Lara, Dietz, Karl‐Josef
Format: Article
Language:English
Subjects:
Cytosol
Electrons
Glutathione
Glutathione peroxidase
Hydrogen peroxide
Insulin
Isoforms
Malate dehydrogenase
Peroxidase
Peroxides
Proteins
Reductases
Reduction
Redundancy
Regeneration
Substrates
Thioredoxin
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Summary:Three soluble type two peroxiredoxins (PRXIIB, C, D) and two glutathione peroxidase‐like enzymes (GPXL2, 8) reside in the cytosol of Arabidopsis thaliana cells and function both as thiol‐dependent antioxidants and redox sensors. Their primary substrate is H2O2, but they also accept other peroxides with a distinct preference between PRXII and GPXL. Less known is their regeneration specificity in the light of the large set of thiol reductases, namely eight annotated thioredoxin h isoforms (TRXh1‐5, 7–9), a few TRX‐like proteins, including CxxS1 (formerly TRXh6) and several glutaredoxins (GRX) associated with the cytosol. This study addressed this open question by in vitro enzyme tests using recombinant protein. GPXL2 and 8 exclusively accepted electrons from the TRX system, namely TRXh1‐5 and TDX, while PRXIIB/C/D were efficiently regenerated with GRXC1 and C2 but not the TRX‐like protein Picot1. They showed significant but low activity (
ISSN:0031-9317
1399-3054
DOI:10.1111/ppl.14042