Glutathione Peroxidase
Scientists at University of Padova, Department of Biological Chemistry release new data on glutathione peroxidase
Published in Proteomics Weekly, February 19th, 2007
New research, "The thioredoxin specificity of Drosophila GPx: a paradigm for a peroxiredoxin-like mechanism of many glutathione peroxidases," is the subject of a report. According to recent research published in the journal JMB Online, "Some members of the glutathione peroxidase (GPx) family have been reported to accept thioredoxin as reducing substrate. However, the selenocysteine-containing ones oxidise thioredoxin (Trx), if at all, at extremely slow rates."
"In contrast, the Cys homolog of Drosophila melanogaster exhibits a clear preference for Trx, the net forward rate constant, k'(+2), for reduction by Trx being 1.5x106 M(-1) s(-1), but...
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Source: Proteomics Weekly (2007-02-19)
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