Kinetics and redox regulation of Gpx1, an atypical 2-Cys peroxiredoxin, in Saccharomyces cerevisiae.
The budding yeast Saccharomyces cerevisiae has three homologues of glutathione peroxidase (GPX1, GPX2, and GPX3). Two structural homologues of the mammalian glutathione peroxidase, Gpx2 and Gpx3, have been proven to be atypical 2-Cys peroxiredoxins, which prefer to use thioredoxin as an electron donor. Here, we show that Gpx1 is also an atypical 2-Cys peroxiredoxin, but uses glutathione and thioredoxin almost equally. We determined the redox state of Gpx1 in vivo.
Ohdate
Takumi
T
Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Kita
Keiko
K
Inoue
Yoshiharu
Y
D015971:Gene Expression Regulation, Enzymologic; D015966:Gene Expression Regulation, Fungal; D005978:Glutathione / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D013879:Thioredoxins / Q000378:metabolism; D000094765:Glutathione Peroxidase GPX1
D029701:Saccharomyces cerevisiae Proteins; D013879:Thioredoxins; D005979:Glutathione Peroxidase; D005978:Glutathione; D000094765:Glutathione Peroxidase GPX1