Thioredoxins function as deglutathionylase enzymes in the yeast <Emphasis Type="Italic">Saccharomyces cerevisiae</Emphasis> |
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Authors: | Darren Greetham Jill Vickerstaff Daniel Shenton Gabriel G Perrone Ian W Dawes Chris M Grant |
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Institution: | (1) Faculty of Life Sciences, The University of Manchester, Manchester, M13 9PT, UK;(2) School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, 2052, Australia |
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Abstract: | Background Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by
protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins
are key oxidoreductases which have been implicated in regulating glutathionylation/deglutathionylation in diverse organisms.
Glutaredoxins have been proposed to be the predominant deglutathionylase enzymes in many plant and mammalian species, whereas,
thioredoxins have generally been thought to be relatively inefficient in deglutathionylation. |
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